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05-184-AF488

MilliporeSigma™ Mouse anti-Src, Clone: GD11, Alexa Fluor 488,

Manufacturer: MilliporeSigma™

Select a Size

Pack Size SKU Availability Price
Each of 1 05-184-AF488-Each-of-1 In Stock ₹ 54,737.67

05-184-AF488 - Each of 1

₹ 54,737.67

In Stock

Quantity

1

Base Price: ₹ 54,737.67

GST (18%): ₹ 9,852.781

Total Price: ₹ 64,590.451

Antigen

Src

Classification

Monoclonal

Conjugate

Alexa Fluor 488

Gene Accession No.

P00526

Host Species

Mouse

Purification Method

Protein G Purified

Regulatory Status

RUO

Primary or Secondary

Primary

Target Species

Avian, Human, Mink, Mouse, Rat

Form

Purified

Applications

Immunocytochemistry

Clone

GD11

Formulation

Purified mouse monoclonal IgG1 antibody conjugate in PBS with 15mg/mL BSA and 0.1% sodium azide.

Gene Symbols

V-SRC; SRC

Immunogen

Recombinant PrA-RSV p60src.

Quantity

100 μL

Research Discipline

Cell Structure

Gene ID (Entrez)

P00526.3

Content And Storage

Stable for one year at 2°C to 8°C from date of receipt.

Isotype

IgG1

Description

  • Specifically detects Src clone: GD11 in Avian, Human, Mink, Mouse, Rat samples, and it is validated for Immunocytochemistry Tyrosine-protein kinase transforming protein Src (EC 2.7.10.2; UniProt P00526; also known as p60-Src, pp60v-src, v-Src) is encoded by the V-SRC gene (Gene ID 1491925) of Rous sarcoma virus strain Prague C (RSV-PrC)
  • Rous sarcoma virus (RSV) V-SRC gene is the first retroviral oncogene discovered
  • V-SRC encodes the v-Src tyrosine kinase that transforms infected host cells into uncontrolled mitosis, providing abundant cells for fresh infection
  • The non-oncogenic chicken c-Src (cellular Src) gene structurally related to v-Src was discovered later in 1979 by J
  • Michael Bishop and Harold E
  • Varmus
  • It is believed that RSV originally took up the chicken proto-oncogene SRC (Gene ID 396442; UniProt P00523) and incorporated into its genome in the mutated concogene form
  • c-Src contains six functional regions, Src homology 4 (SH4) domain, unique region, SH3 domain, SH2 domain, catalytic domain, and short regulatory tail
  • In its inactive state, Src is phosphorylated at Tyr527
  • The pTyr527 interacts with the SH2 domain which helps the SH3 domain interact with the linker domain and consequently keeps the inactive unit tightly bound
  • Dephosphorylation of pTyr527 destabilizes the inactive conformation, opening up the SH3, SH2 and the kinase domains, leading to Tyr416 autophosphorylation and c-Src activation.