Sperm Mitochondrial-Associated Cysteine-Rich Protein (SMCP) Antibody

292.5€ (80 µl)
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935106861
info@markelab.com
name
Sperm Mitochondrial-Associated Cysteine-Rich Protein (SMCP) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx027039
tested applications
ELISA, WB
Description
Sperm mitochondria differ in morphology and subcellular localization from those of somatic cells. They are elongated, flattened, and arranged circumferentially to form a helical coiled sheath in the midpiece of the sperm flagellum. The protein encoded by this gene localizes to the capsule associated with the mitochondrial outer membranes and is thought to function in the organization and stabilization of the helical structure of the sperm's mitochondrial sheath.
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | Sperm Mitochondrial-Associated Cysteine-Rich Protein (SMCP) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified through a protein A column, followed by peptide affinity purification. |
Size 1 | 80 µl |
Size 2 | 400 µl |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS containing 0.09% sodium azide. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | P49901 |
Background | Antibody anti-SMCP |
Status | RUO |
Descripción
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Sperm Mitochondrial-Associated Cysteine-Rich Protein (SMCP) Antibody
Sperm mitochondria differ in morphology and subcellular localization from those of somatic cells. They are elongated, flattened, and arranged circumferentially to form a helical coiled sheath in the midpiece of the sperm flagellum. The protein encoded by this gene localizes to the capsule associated with the mitochondrial outer membranes and is thought to function in the organization and stabilization of the helical structure of the sperm's mitochondrial sheath.
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