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MME antibody (Membrane Metallo-Endopeptidase) (AA 274-302)

Details for Product anti-MME Antibody No. ABIN391500, Supplier: Log in to see
Antigen
  • MME
  • NEP
  • CD10
  • CALLA
  • CAK
  • CD167
  • DDR
  • EDDR1
  • HGK2
  • MCK10
  • NTRK4
  • PTK3
  • PTK3A
  • RTK6
  • TRKE
  • AV378681
  • Mmel
  • 6030454K05Rik
  • C85356
  • SFE
  • Nep
Alternatives
anti-Human MME antibody for Immunoprecipitation
Epitope
AA 274-302, Center
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19
19
16
14
11
6
6
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6
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5
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3
3
3
3
3
3
2
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2
2
2
2
2
2
1
1
1
1
1
Reactivity
Human, Mouse (Murine)
457
61
61
2
1
1
Host
Rabbit
303
169
2
Clonality (Clone)
Polyclonal ()
Conjugate
This MME antibody is un-conjugated
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42
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6
5
3
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2
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2
2
2
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1
1
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1
1
1
Application
Immunofluorescence (IF), Western Blotting (WB)
214
195
118
111
77
59
51
46
26
13
12
8
5
4
3
2
2
2
1
1
Supplier
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Immunogen This MME antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 274-302 AA from the Central region of human MME.
Clone RB18820
Isotype Ig
Specificity This MME antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 281~310 amino acids from the Center region of human MME.
Predicted Reactivity Rat (Rattus)
Purification This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Alternative Name MME (MME Antibody Abstract)
Background MME is a common acute lymphocytic leukemia antigen that is an important cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). This protein is present on leukemic cells of pre-B phenotype, which represent 85% of cases of ALL. This protein is not restricted to leukemic cells, however, and is found on a variety of normal tissues. It is a oprotein that is particularly abundant in kidney, where it is present on the brush border of proximal tubules and on glomerular epithelium. The protein is a neutral endopeptidase that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin.
Synonyms: Neprilysin, Neutral endopeptidase 24.11, Neutral endopeptidase, NEP, Enkephalinase, Atriopeptidase, Common acute lymphocytic leukemia antigen, CALLA, CD_antigen=CD10, EPN, MME
Molecular Weight 85514 DA
Gene ID 4311
UniProt P08473
Research Area Cell Structure
Pathways RTK Signaling
Application Notes WB = 1:1000, IF = 1:10-50
Restrictions For Research Use only
Format Liquid
Concentration 2 mg/mL
Buffer PBS with 0.09 % (W/V) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Expiry Date 6 months
Supplier Images
Western Blotting (WB) image for anti-MME antibody (Membrane Metallo-Endopeptidase) (AA 274-302) (ABIN391500) Western blot analysis of Neprilysin antibody (Center) (ABIN391500) in mouse kidney ti...
Background publications Dakka, Bellaoui, Bouzid et al.: "CD10 AND CD34 expression in childhood acute lymphoblastic leukemia in Morocco: clinical relevance and outcome." in: Pediatric hematology and oncology, Vol. 26, Issue 4, pp. 216-31, 2009 (PubMed).

Wang, Wang, Malter et al.: "Effects of HNE-modification induced by Abeta on neprilysin expression and activity in SH-SY5Y cells." in: Journal of neurochemistry, Vol. 108, Issue 4, pp. 1072-82, 2009 (PubMed).

Shipp, Vijayaraghavan, Schmidt et al.: "Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): direct evidence by cDNA transfection analysis." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, Issue 1, pp. 297-301, 1989 (PubMed).

Shipp, Tarr, Chen et al.: "CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 23, pp. 10662-6, 1992 (PubMed).