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Safety Information

AV44235

Sigma-Aldrich

Anti-SHH antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-HHG1, Anti-HLP3, Anti-HPE3, Anti-SMMCI, Anti-Sonic hedgehog homolog (Drosophila), Anti-TPT, Anti-TPTPS

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About This Item

UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

mol wt

28 kDa

species reactivity

canine, horse, rat, mouse, rabbit, human, guinea pig, zebrafish

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... SHH(6469)

General description

Sonic hedgehog homolog (Drosophila) (SHH, HHG1, HLP3, HPE3, SMMCI, TPTPS) is a cell signaling protein, morphogen, involved in vertebrate organogenesis wherein it regulates the growth of limbs and the organization and patterning of CNS and brain structures. SHH initiates hedgehog cell signaling via its interaction with Gli family proteins.

Specificity

Anti-SHH polyclonal antibody reacts with mouse, human, zebrafish, chicken, rat, and canine sonic hedgehog homolog (Drosophila) proteins.

Immunogen

The immunogen for anti-SHH antibody: synthetic peptide derected towards the N terminal of human SHH

Application

Anti-SHH polyclonal antibody is used to tag sonic hedgehog homolog (Drosophila) for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of sonic hedgehog homolog (Drosophila) developmental processes such as CNS patterning and limb growth and organization.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Sequence

Synthetic peptide located within the following region: RCLLLVLVSSLLVCSGLACGPGRGFGKRRHPKKLTPLAYKQFIPNVAEKT

Physical form

Lyophilized from PBS buffer with 2% sucrose

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Rory L Cooper et al.
Evolution & development, 25(1), 54-72 (2023-01-04)
Vertebrate skin appendages are incredibly diverse. This diversity, which includes structures such as scales, feathers, and hair, likely evolved from a shared anatomical placode, suggesting broad conservation of the early development of these organs. Some of the earliest known skin
Katsunori Nochioka et al.
Acta histochemica et cytochemica, 49(2), 67-74 (2016-05-31)
Choroidal neovascularization is one of the major pathological changes in age-related macular degeneration, which causes devastating blindness in the elderly population. The molecular mechanism of choroidal neovascularization has been under extensive investigation, but is still an open question. We focused
Vivien Jane Coulson-Thomas et al.
The Journal of biological chemistry, 289(36), 25211-25226 (2014-07-24)
Hair follicle (HF) morphogenesis and cycling are a result of intricate autonomous epithelial-mesenchymal interactions. Once the first HF cycle is complete it repeatedly undergoes cyclic transformations. Heparan sulfate (HS) proteoglycans are found on the cell surface and in the extracellular
Hong-Xing Dang et al.
International journal of molecular medicine, 40(1), 209-216 (2017-06-01)
The aim of this study was to examine the effect of calcitonin gene-related peptide (CGRP) on primary alveolar epithelial type II (AECII) cells and expression of Sonic hedgehog (SHH) signaling pathway components following exposure to hyperoxia. The AECII cells were isolated and purified from

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