ANXA7 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P20073 |
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Clone Names | 90819124 |
Gene ID | 310 |
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Other Names | Annexin A7, Annexin VII, Annexin-7, Synexin, ANXA7, ANX7, SNX |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8738c was selected from the Center region of human ANXA7. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | ANXA7 |
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Synonyms | ANX7, SNX |
Function | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. |
Tissue Location | Isoform 1 is expressed in brain, heart and skeletal muscle. Isoform 2 is more abundant in liver, lung, kidney, spleen, fibroblasts and placenta. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins.The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in two mRNA transcripts of 2.0 and 2.4 kb which are predicted to generate two protein isoforms differing in their N-terminal domain. ANXA7 is a protein with a molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties, including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.
References
Shirvan,A., et.al., Biochemistry 33 (22), 6888-6901 (1994)
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