PIMA526932

Kindlin 3 Monoclonal Antibody (OTI2G2), Invitrogen™

Manufacturer: Thermo Scientific

Select a Size

Pack Size SKU Availability Price
Each of 1 PIMA526932-Each-of-1 In Stock ₹ 52,198.50

PIMA526932 - Each of 1

₹ 52,198.50

In Stock

Quantity

1

Base Price: ₹ 52,198.50

GST (18%): ₹ 9,395.73

Total Price: ₹ 61,594.23

Antigen

Kindlin 3

Classification

Monoclonal

Concentration

1 mg/mL

Formulation

PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3

Gene Accession No.

Q86UX7

Gene Symbols

Fermt3

Immunogen

Human recombinant protein fragment corresponding to amino acids 259-528 of FERMT3 produced in E.coli

Quantity

100μL

Primary or Secondary

Primary

Target Species

Human

Product Type

Antibody

Isotype

IgG2b

Applications

Immunohistochemistry (Paraffin), Western Blot

Clone

OTI2G2

Conjugate

Unconjugated

Gene

Fermt3

Gene Alias

C79673; fermitin family homolog 3; fermitin family homolog 3 (Drosophila); fermitin family member 3; Fermt3; Kind3; kindlin 3; Kindlin3; Kindlin-3; MGC10966; MIG-2; MIG2B; MIG2-like protein; RGD1310168; UNC-112 related protein 2; UNC112C; unc-112-related protein 2; URP2; URP2SF

Host Species

Mouse

Purification Method

Affinity Chromatography

Regulatory Status

RUO

Gene ID (Entrez)

83706

Content And Storage

-20° C, Avoid Freeze/Thaw Cycles

Form

Liquid

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Description

  • The three KINDLINs are a novel family of focal adhesion proteins, localizing to integrin adhesion sites
  • The KINDLIN proteins are composed of a centrally located FERM domain interrupted by a pleckstrin homology (PH) domain
  • KINDLIN1 and KINDLIN2 have been shown to play an essential role in integrin-mediated adhesion and spreading
  • In contrast to the widely expressed KINDLIN1 and KINDLIN2, KINDLIN3 is restricted to hematopoietic cells and is particularly abundant in megakaryocytes and platelets
  • Several reports describe a transcriptional misregulation of KINDLINs in various types of cancer
  • A recent study demonstrates that KINDLIN3 is essential for platelet integrin activation and subsequent integrin outside-in signaling, suggesting it may serve as a potential target for the design of therapeutics aimed at specifically disrupting integrin activation in platelets and leukocytes.