anti-s100-a1 (S10A1) Antibodies

The protein encoded by S10A1 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. Additionally we are shipping s100-a1 Proteins (1) and many more products for this protein.

list all antibodies Gene Name GeneID UniProt
S10A1 6271 P23297
S10A1 20193 P56565
S10A1 295214 P35467
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Top anti-s100-a1 Antibodies at

Showing 4 out of 4 products:

Catalog No. Reactivity Host Conjugate Application Images Quantity Supplier Delivery Price Details
Cow Rabbit Un-conjugated IC, IF, WB Immunofluorescent analysis of S100-A1 staining in HEK293T cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 °C in a humidified chamber. Cells were washed with PBST and incubated with a DyLight 594-conjugated secondary antibody (red) in PBS at room temperature in the dark. DAPI was used to stain the cell nuclei (blue). Western blot analysis of S100-A1 expression in HEK293T (A), mouse brain (B), rat brain (C), C6 (D) whole cell lysates. 200 μL Log in to see 13 to 14 Days
Cow Rabbit Un-conjugated IHC, WB Immunohistochemical analysis of S100-A1 staining in human brain formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the Western blot analysis of S100-A1 expression in Hela (A) whole cell lysates. 200 μL Log in to see 13 to 14 Days
Human Rabbit Un-conjugated IHC, WB   200 μL Log in to see 13 to 14 Days
Human Rabbit Un-conjugated WB   100 μL Log in to see 10 to 11 Days

More Antibodies against s100-a1 Interaction Partners

Human s100-a1 (S10A1) interaction partners

  1. Data suggest that TRPM4 exhibits binding sites for calmodulin (CaM) and S100 calcium-binding protein A1 (S100A1) located in very distal part of TRPM4 N-terminus. (TRPM4 = transient receptor potential cation channel subfamily M member 4)

  2. Data found that S100A1 was upregulated in hepatocellular carcinoma (HCC) tissues, and its upregulation was associated with large tumor size, low differentiation, and shorter survival rates. Further results supports the hypothesis that S100A1 functions as an oncogene and may be a biomarker for the prognosis of patients with HCC. S100A1 exerted its oncogenic function by interacting with LATS1 and activating Hippo pathway.

  3. The results indicate that changes in the circulating level of S100A1 protein occur in metabolic syndrome patients. The strong correlation between serum zinc-alpha2-glycoprotein and S100A1 might suggest that production or release of these two proteins could be related mechanistically.

  4. The results indicated that S100A1 enhanced the ovarian cancer cell proliferation and migration.

  5. found that S100B plays a crucial role in blocking the interaction site between RAGE V domain and S100A1. A cell proliferation assay WST-1 also supported our results. This report could potentially be useful for new protein development for cancer treatment

  6. Study provides evidence that mir-363 and its target S100A1 are under the regulatory function of FOXD2-AS1 aggravating nasopharyngeal carcinoma carcinogenesis.

  7. X-ray crystal structure of human calcium-bound S100A1 has been reported.

  8. a molecular mechanism for the potential regulation of TRPM1 by S100A1

  9. Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 are key players in this pathway; the stoichiometry of S100A1/STIP1 interaction appears to be three S100A1 dimers plus one STIP1 monomer; each S100A1-STIP1-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 = stress-induced-phosphoprotein 1) [REVIEW]

  10. Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1.

  11. Results identified amino acids motif in S100A1 for protein binding to 2-oxohistidine which appears to be an evolutionarily conserved capacity from bacteria to human.

  12. a correlation between S100B + A1-positive Human Articular Chondrocytes in monolayer culture and their neochondrogenesis capacity in pellet culture, is reported.

  13. CaM and S100A1 can concurrently bind to and functionally modulate RyR1 and RyR2, but this does not involve direct competition at the RyR CaM binding site.

  14. In line with these observations, rhesus monkey rhadinovirus infection resulted in rapid degradation of SP100, followed by degradation of PML and the loss of ND10 structures, whereas the protein levels of ATRX and DAXX remained constant.

  15. High Serum protein S100 levels are associated with postoperative delirium after off-pump coronary artery bypass surgery.

  16. molecular dynamics simulations of S100A1 in the apo/holo (Ca(2+)-free/bound) states, is reported.

  17. The relationship between the degree of infiltration by S100-positive (S100+) dendritic cells and prognostic factors, including histological subtype, histological grade, peritumor inflammatory infiltration, and stromal desmoplasia, were examined.

  18. In this review, we aim to describe the molecular basis and regulatory function of S100A1--{REVIEW}

  19. Data indicate that Cu-oxidized S100 calcium binding protein A4 (S100A4) interacted with S100 calcium binding protein A1 (S100A1) and prevented protein phosphatase 5 (PP5) activation.

  20. Patients with acute myocardial infarction (MI) showed significantly increased S100A1 serum levels. S100A1 signaling in cardiac fibroblasts occurs through endosomal TLR4/MyD88.

Cow (Bovine) s100-a1 (S10A1) interaction partners

  1. identified S100A1, but not calmodulin or other S100 proteins, as a potent molecular chaperone and a new member of the Hsp70/Hsp90 multichaperone complex (S100A1)

  2. Results suggest that S100A1 can act as a linker between the calcium and redox signalling pathways.

  3. beta-mercaptoethanol modification of apo-S100A1 makes its structure more similar to that of holo-S100A1, so that it becomes much better adjusted for calcium coordination.

Mouse (Murine) s100-a1 (S10A1) interaction partners

  1. Data (including data from studies using knockout mice) suggest that S100A1 (S-100 calcium-binding protein A1, alpha chain) is involved in protein kinase A- (RIIalpha and RIIbeta)-dependent signaling resulting in nuclear redistribution/influx of HDAC4 (histone deacetylase 4) in skeletal muscle fibers.

  2. S100A1-KO exhibited increased right ventricular (RV) weight and elevated RV pressure in the absence of altered left ventricular filling pressures, increase in wall thickness of muscularized pulmonary arteries and a reduction in microvascular perfusion.

  3. S100A1 and S100B are dispensable for endochondral ossification during skeletal development.

  4. S100A1 ablationalso reduced plaque associated and increased non-plaque associated PO4-Akt and PO4-GSK3beta staining.

  5. Patients with acute myocardial infarction (MI) showed significantly increased S100A1 serum levels. Experimental MI in mice induced comparable S100A1 release. S100A1 signaling in cardiac fibroblasts occurs through endosomal TLR4/MyD88.

  6. hypoxia-induced MiR-138 is an essential mediator of EC dysfunction via its ability to target the 3'UTR of S100A1.

  7. Report downregulation of S100A1 expression in critical limb ischemia impairs postischemic angiogenesis via compromised proangiogenic endothelial cell function and nitric oxide synthase regulation.

  8. S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor type 1 to tune the Ca2+ release process, and thereby regulate skeletal muscle function. (Review)

  9. The RyR1-L3625D mutation removed both an early activating effect of S100A1 and calmodulin and delayed the suppression of RyR1 Ca2+ release, providing new insights into calmodulin and S100A1 regulation of skeletal muscle excitation-contraction coupling.

  10. Data suggest that the absence of S100A1 suppresses physiological AP-induced Ca(2+) release flux, resulting in impaired contractile activation and force production in skeletal muscle.

  11. Chronic absence of S100A1 results in enhanced L-type Ca2+ channel activity combined with a blunted sarcoplasmic reticulum Ca2+ release amplification.

  12. may serve as an endogenous enhancer of sarcoplasmic reticulum Ca2+ release and might therefore be of physiological relevance in the process of excitation-contraction coupling in skeletal muscle

  13. S100A1 plays an important in vivo role in the regulation of cardiac function perhaps through interacting with the ryanodine receptor

  14. S100A1 is a calcium binding protein that augments transsarcolemmal Ca2+ influx via an increase of PKA activity in ventricular cardiomyocytes, regulating cardiac function

  15. study provides evidence that downregulation of S100A1 protein critically contributes to contractile dysfunction of the diseased heart, which is potentially responsible for driving the progressive downhill clinical course to postischemic heart failure

  16. S100A1 plays a role in modulating innate fear and exploration of novel stimuli.

  17. Ca(2+)-dependent interaction of S100A1 with Atpaf1 leads to an increased ATP content in cardiomyocytes.

  18. S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling

  19. Endothelial S100A1 modulates vascular function because lack of S100A1 expression leads to decreased endothelial NO release, which contributes to impaired endothelium-dependent vascular relaxation and hypertension in SKO mice.

  20. S100A1 deficiency results in cardiac repolarization delay and alternating ventricular conduction defects in response to sympathetic activation accompanied by a significantly different transcriptional regulation.

s100-a1 (S10A1) Antigen Profile

Protein Summary

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of this protein has been implicated in cardiomyopathies.

Gene names and symbols associated with anti-s100-a1 (S10A1) Antibodies

  • S100 calcium binding protein A1 (S100A1) antibody
  • S100 calcium binding protein A1 (S100a1) antibody
  • AI266795 antibody
  • S100 antibody
  • S100-alpha antibody
  • S100a antibody

Protein level used designations for anti-s100-a1 (S10A1) Antibodies

S-100 protein alpha chain , S-100 protein subunit alpha , S100 alpha , S100 calcium-binding protein A1 , S100 protein, alpha polypeptide , protein S100-A1

100858258 Gallus gallus
6271 Homo sapiens
480141 Canis lupus familiaris
528735 Bos taurus
20193 Mus musculus
295214 Rattus norvegicus
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