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Key Documents

SAB1408633

Sigma-Aldrich

Anti-TAGLN antibody produced in rabbit

purified immunoglobulin, buffered aqueous solution

Synonym(s):

DKFZp686P11128, SM22, SMCC, TAGLN1, WS3-10

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~22.6 kDa

species reactivity

human

technique(s)

western blot: 1 μg/mL

NCBI accession no.

NM_001001522.1

UniProt accession no.

Q01995

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TAGLN(6876)

Related Categories

General description

The protein encoded by this gene is a transformation and shape-change sensitive actin cross-linking/gelling protein found in fibroblasts and smooth muscle. Its expression is down-regulated in many cell lines, and this down-regulation may be an early and sensitive marker for the onset of transformation. A functional role of this protein is unclear. Two transcript variants encoding the same protein have been found for this gene. (provided by RefSeq)

Immunogen

TAGLN (NP_001001522.1, 1 a.a. ~ 201 a.a) full-length human protein.

Sequence
MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIIVQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPDGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVIKTDMFQTVDLFEGKDMAAVQRTLMALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTESQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS

Physical form

Solution in phosphate buffered saline, pH 7.4

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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K H Al-Gubory et al.
Reproduction (Cambridge, England), 147(5), 599-614 (2014-01-22)
The expression and regulation of endometrial proteins are crucial for conceptus implantation and development. However, little is known about site-specific proteome profiles of the mammalian endometrium during the peri-implantation period. We utilised a two-dimensional gel electrophoresis/mass spectrometry-based proteomics approach to

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