HSPB1 antibody (Heat Shock 27kDa Protein 1)

Details for Product anti-HSPB1 Antibody No. ABIN222927, Supplier: Log in to see
Antigen
  • CMT2F
  • HMN2B
  • HS.76067
  • HSP27
  • HSP28
  • Hsp25
  • SRP27
  • 27kDa
  • Hsp27
  • cb153
  • cb660
  • hsp1
  • hsp25
  • hsp27
  • id:ibd2821
  • sb:cb660
  • zgc:103437
  • HSPB1
  • cmt2f
  • hs.76067
  • hsp28
  • heat shock protein family B (small) member 1
  • heat shock protein 1
  • heat shock protein, alpha-crystallin-related, 1
  • heat shock protein family B (small) member 1 L homeolog
  • HSPB1
  • Hspb1
  • hspb1
  • hspb1.L
Alternatives
anti-Human HSPB1 antibody for ELISA
Reactivity
Human, Monkey
821
276
271
96
85
71
68
66
35
30
29
26
18
11
11
9
6
3
2
2
2
2
1
1
1
Host
Rabbit
501
338
2
Clonality
Polyclonal
Conjugate
This HSPB1 antibody is un-conjugated
34
32
22
21
19
13
13
13
11
11
10
10
10
10
10
9
9
9
5
5
5
5
5
5
5
5
5
4
4
3
3
3
3
3
3
3
3
3
3
3
2
Application
Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
711
327
270
266
227
212
168
156
59
40
17
14
11
8
6
4
2
2
1
1
1
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Immunogen Recombinant human Hsp27
Isotype IgG
Specificity The antibody detects a 27 kDa protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, dog (weakly) and pig (weakly) origins.
Purification Affinity purified
Alternative Name Hsp27 (HSPB1 Antibody Abstract)
Background Human Hsp27, mouse Hsp25 and αβ-crystallin are part of a diverse family of small heat shock proteins which are produced in all organisms. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. Hsp27 is believed to exist mainly as oligomers of as many as 8-40 Hsp27 protein monomers in cells and data sμggests that the large oligomers of Hsp27 have a chaperone-like activity by serving as a site where unfolding proteins may bind until ATP and Hsp70-dependent refolding can occur. Hsp27 is believed to protect cells by enhancing cellular glutathione levels and elevated glutathione levels have been measured in cells overexpressing Hsp27. Data from studies using wild-type Hsp27 and mutant forms in which the serine phosphorylation sites were mutated to alanines, glycines or aspartates, have shown that cellular glutathione levels depend on the oligomerization of Hsp27. Recent findings indicate that Hsp27 is also a negative regulator of cytochrome c-dependent activation of procaspase-3.
Synonyms: HSPB1, CMT2F, DKFZp586P1322, HS.76067, HSP27, HSP28, Hsp25
Gene ID 11036357
Research Area Cardiovascular, Contractility, Atherosclerosis, Heat Shock Proteins, Cytoskeleton, Microfilaments
Pathways MAPK Signaling, Regulation of Actin Filament Polymerization, Signaling Events mediated by VEGFR1 and VEGFR2, Negative Regulation of intrinsic apoptotic Signaling, VEGF Signaling
Application Notes Western blotting (1-2 μg/mL), immunoprecipitation (5-10 μg/mL), immunocytochemistry (10-15 μg/mL), and ELISA (1 μg/mL). However, the optimal conditions should be determined individually. The antibody detects a 27 kDa protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, dog (weakly) and pig (weakly) origins.
Restrictions For Research Use only
Format Liquid
Concentration 0.2 mg/mL
Buffer 100 μg (200 μg/mL) in phosphate buffered saline (PBS), pH 7.2, containing 50 % glycerol, 1 % BSA, 0.02 % thimerosal.
Preservative Thimerosal (Merthiolate)
Precaution of Use This product contains Thimerosal (Merthiolate): a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice The antibody solution should be gently mixed before use.
Storage -20 °C
Storage Comment For long-term storage, aliquot and freeze at -70 °C.
Expiry Date 12 months
Product cited in: Cheng, Pollock, Mahimkar, Olson, Lovett: "Matrix metalloproteinase 2 and basement membrane integrity: a unifying mechanism for progressive renal injury." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 20, Issue 11, pp. 1898-900, 2006 (PubMed).

Did you look for something else?