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Recombinant Human AFAP protein (denatured) is a Human Fragment protein, in the 250 to 590 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.

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Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

Biologically active

No

Sequence

M G S S H H H H H H S S G L V P R G S H M G C S G P V D S E C P P P P S S P V H K A E L E K K L S S E R P S S D G E G V V E N G I T T C N G K E Q V K R K K S S K S E A K G T V S K V T G K K I T K I I S L G K K K P S T D E Q T S S A E E D V P T C G Y L N V L S N S R W R E R W C R V K D N K L I F H K D R T D L K T H I V S I P L R G C E V I P G L D C K H P L T F R L L R N G Q E V A V L E A S S S E D M G R W I G I L L A E T G S S T D P E A L H Y D Y I D V E M S A S V I Q T A K Q T F C F M N R R V I S A N P Y L G G T S N G Y A H P S G T A L H Y D D V P C I N G S L R G K K P P V A S N G V T G K G K T L S S Q P K K A D P A A V V K R T G S N A A Q Y K Y G K N R V E A D A K R L Q T K E E E L L K R K E A L R N R L A Q L R K

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Shipping To:
United States

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Images

Target data

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Recombinant Human AFAP protein (denatured) is a Human Fragment protein, in the 250 to 590 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Applications

SDS-PAGE

Predicted molecular weight

39.5 kDa

Amino acids

250 to 590

Sequence

M G S S H H H H H H S S G L V P R G S H M G C S G P V D S E C P P P P S S P V H K A E L E K K L S S E R P S S D G E G V V E N G I T T C N G K E Q V K R K K S S K S E A K G T V S K V T G K K I T K I I S L G K K K P S T D E Q T S S A E E D V P T C G Y L N V L S N S R W R E R W C R V K D N K L I F H K D R T D L K T H I V S I P L R G C E V I P G L D C K H P L T F R L L R N G Q E V A V L E A S S S E D M G R W I G I L L A E T G S S T D P E A L H Y D Y I D V E M S A S V I Q T A K Q T F C F M N R R V I S A N P Y L G G T S N G Y A H P S G T A L H Y D D V P C I N G S L R G K K P P V A S N G V T G K G K T L S S Q P K K A D P A A V V K R T G S N A A Q Y K Y G K N R V E A D A K R L Q T K E E E L L K R K E A L R N R L A Q L R K

Accession
Q8N556-1
Protein length

Fragment

Animal free

No

Nature

Recombinant

Species

Human

Concentration
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Storage buffer

pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl

Specifications

Form

Liquid

Additional notes

ab181922 is purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.

General info

Function

Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.

Post-translational modifications

Phosphorylated on tyrosine residues by SRC.

Subcellular localisation

Cytoskeleton, Stress fiber

Storage

Shipped at conditions

Blue Ice

Appropriate short-term storage duration

1-2 weeks

Appropriate short-term storage conditions

+4°C

Appropriate long-term storage conditions

-20°C

Aliquoting information

Upon delivery aliquot

Storage information

Avoid freeze / thaw cycle

Product promise

We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.

In the unlikely event of one of our products not working as expected, you are covered by our product promise.

Full details and terms and conditions can be found here:
Terms & Conditions.

Downloads

Product protocols

For this product, it's our understanding that no specific protocols are required. You can:

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

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