Search: 1000 results found for "anti mouse cytokine"

Description:

Interleukin-36 Gamma (152 a.a) Human Recombinant

Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.

Product # :

CYT-161

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Description

IL36G (152 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.0kDa.The IL36G (152 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4, containing 5% trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-8 secretion in human preadipocytes is less than 15ng/ml, corresponding to a Specific Activity of 67,000 IU/mg.

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Introduction
IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and IL-1F10. ). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.
Synonyms
Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36g Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Resistin Rat Recombinant

Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Product # :

CYT-1129

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Description

Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Beta Defensin-3 Rat Recombinant

Beta-defensin 3, BD-3, Defensin beta 3, Defb3.

Product # :

CYT-063

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Description

BD-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.5kDa.The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-3 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Measured by its antimicrobial activity against E. coli. The ED₅₀ for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BD-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BD-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
Background
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 4.5kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

What is the amino acid sequence of BD3 Protein?
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-1 alpha Human Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-253

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Shipped at Room temp

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Description

Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM Tris-HCl, pH 8.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 10⁹ IU/mg.

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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.
Background
What is the molecular weight/Mw of IL1A HUMAN Protein?
IL1A HUMAN Protein has a total Mw of 18kDa.

What is the source or expression system of IL1A HUMAN Protein?
Escherichia Coli.

What is the Purity of IL1A HUMAN Protein?
IL1A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

What is the amino acid sequence of IL1A HUMAN Protein?
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

What applications can IL1A HUMAN Protein be used in?
IL1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A HUMAN Protein?
The endotoxin level is minimal, IL1A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-3 Canine Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-722

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Description

Interleukin-3 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 14 kDa. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 1X PBS pH7.4.

Purity

Greater than 97.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.
Background
What is the molecular weight/Mw of IL 3 DOG Protein?
IL 3 DOG Protein has a total Mw of 14kDa.

What is the source or expression system of IL 3 DOG Protein?
Escherichia Coli.

What is the Purity of IL 3 DOG Protein?
IL 3 DOG Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 DOG Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

What is the amino acid sequence of IL 3 DOG Protein?
RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.

What applications can IL 3 DOG Protein be used in?
IL 3 DOG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 DOG Protein?
The endotoxin level is minimal, IL 3 DOG Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 DOG that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 DOG?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-4 Human Recombinant

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-211

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Shipped at Room temp

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Description

Interleukin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15kDa. The IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 98% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Everything You Should Know About IL-4 Human Recombinant
Interleukin-4 (IL-4) is an important type-2 cytokine with multiple effects on numerous cells and tissues in the body. As such, it's crucial for the immune system's maintenance and function.
Recent advancements have led to the development of interleukin-4 (rhIL-4) human recombinant in laboratories. As a result, experts have started studying its potential uses and therapeutic applications.
If you're interested in learning more about IL-4 human recombinant, check out the information below!
How Does Interleukin-4 (IL-4) Work?
Interleukin-4 (IL-4) acts as a signaling molecule, specifically a protein. It communicates with various immune cells by binding to specific receptors on their surface.
This process triggers responses against common threats, such as allergens, contaminants, and infections.
IL-4 is produced by T helper 2 (Th2) cells (a type of white blood cells), mast cells, eosinophils, and basophils.
What Interleukin-4 (IL-4) Does
As mentioned, this type-2 cytokine has multiple effects on various cells and tissues, so it fulfills several functions. Below are the most important ones:
- Th2 cell differentiation: IL-4 promotes the differentiation of T cells, triggering the response of Th2 cells, which fight parasites and regulate allergic responses.
- B cell activation and antibody production: IL-4 stimulates B cells, helping them proliferate and produce antibodies, particularly immunoglobulin E (IgE), which is involved in allergic reactions.
- Inflammation reduction: IL-4 can promote inflammation to address threats, such as allergens or parasites, and suppress it when necessary, depending on the context.
- Tissue repair and remodeling: IL-4 is key for tissue repair and remodeling processes, such as wound healing and fibrosis.
What Is IL-4 Human Recombinant?
IL-4 human recombinant is a version produced in a laboratory using DNA technology. The cytokine is inserted into a host organism, commonly E. Coli bacteria, for mass production.
This method allows experts to obtain pure and contaminant-free rhIL-4 with uniform biological activity and in large quantities.
What Can IL-4 Human Recombinant Be Used For?
Since this cytokine plays a key role in different processes, it may have multiple therapeutic applications for numerous diseases. These are the most common:
- Allergic diseases, such as asthma, rhinitis, and eczema
- Autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis
- Infectious diseases, including those caused by parasites and viruses
- Cancer, as research suggests IL-4 could enhance the immune system's ability to fight cancer cells
Final Thoughts
The future of IL-4 human recombinant seems promising. This laboratory-produced version of an essential type-2 cytokine may be key to developing innovative therapies. However, more research is needed on potential applications to determine if it's safe and effectiv.
What is the molecular weight/Mw of IL 4 HUMAN Protein?
IL 4 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IL 4 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL 4 HUMAN Protein?
IL 4 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

What is the amino acid sequence of IL 4 HUMAN Protein?
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.

What applications can IL 4 HUMAN Protein be used in?
IL 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 HUMAN Protein?
The endotoxin level is minimal, IL 4 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 4 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.594 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-4 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Flt3-Ligand Rhesus Macaque Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-157

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Flt3 Ligand Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 18.0kDa.The Flt3 Ligand Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3 Ligand Rhesus Macaque although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3 Ligand Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Flt3 Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
Background
What is the molecular weight/Mw of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein has a total Mw of 18kDa.

What is the source or expression system of FLT3-LIGAND RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3-LIGAND RHESUS MACAQUE Protein?
The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

What is the amino acid sequence of FLT3-LIGAND RHESUS MACAQUE Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
What applications can FLT3-LIGAND RHESUS MACAQUE Protein be used in?
FLT3-LIGAND RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3-LIGAND RHESUS MACAQUE Protein?
The endotoxin level is minimal, FLT3-LIGAND RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth and Differentiation Factor 15 Human Recombinant, His Tag

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-691

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2), His Tag

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

Product # :

CHM-246

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source
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Citations

Description

MCP-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids (24-99) and having a molecular mass of 10.9 kDa. The MCP-1 is fused to 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The His Tag MCP-1 protein (1mg/ml) solution contains 20mM Tris-HCL pH-8.0, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein has a total Mw of 10.9kDa.

What is the source or expression system of CCL2 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HIS Protein?
The biological functionality of CCL2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL2 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.

What applications can CCL2 HUMAN, HIS Protein be used in?
CCL2 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL2 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL2 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Gankyrin, Mouse Anti Human

26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

Product # :

ANT-609

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formulation
More Info
Citations

Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.
Synonyms
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PSMD10 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PSMD10 protein 1-226 amino acids purified from E.coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1F4AT.
Applications
PSMD10 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PSMD10 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Mutase 1 Mouse Recombinant, Active

Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

Product # :

ENZ-980

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Description

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is >150units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.

More Info

Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-23 Receptor Human Recombinant

Interleukin 23 Receptor, IL-23 Receptor, IL-23R, IL23R.

Product # :

CYT-991

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Description

Interleukin-23 Receptor Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (24-355a.a.) and having a molecular mass of 65.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).IL23R is fused with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL23R protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-23 receptor (IL23R) is a member of the type I cytokine receptor family, Type 2 subfamily. IL23R contains two fibronectin type-III domains and is expressed by monocytes, Th1, Th0, NK and dendritic cells. IL23R protein pairs with the receptor molecule IL12RB1/IL12Rbeta1, and both are necessary for IL23A signaling. IL23R protein associates constitutively with JAK2 (Janus kinase 2), and it also binds to transcription activator STAT3 in a ligand-dependent manner. IL23R binds IL23 and mediates T-cells, NK cells and perhaps certain macrophage/myeloid cells stimulation most likely by way of activation of the Jak-Stat signaling cascade. IL23R might be responsible for autoimmune inflammatory diseases and be vital for tumorigenesis.
Synonyms
Interleukin 23 Receptor, IL-23 Receptor, IL-23R, IL23R.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPGITNINC SGHIWVEPAT IFKMGMNISI YCQAAIKNCQ PRKLHFYKNG IKERFQITRI NKTTARLWYK NFLEPHASMY CTAECPKHFQ ETLICGKDIS SGYPPDIPDE VTCVIYEYSG NMTCTWNAGK LTYIDTKYVV HVKSLETEEE QQYLTSSYIN ISTDSLQGGK KYLVWVQAAN ALGMEESKQL QIHLDDIVIP SAAVISRAET INATVPKTII YWDSQTTIEK VSCEMRYKAT TNQTWNVKEF DTNFTYVQQS EFYLEPNIKY VFQVRCQETG KRYWQPWSSL FFHKTPETVP QVTSKAFQHD TWNSGLTVAS ISTGHLTSDN RGDIGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Osteopontin 1 Mouse Recombinant

Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1

Product # :

CYT-1201

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biological activity
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Description

SPP1 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 287 amino acids (17-294 a.a) and having a molecular mass of 31.8kDa.SPP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SPP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by the ability of the immobilized protein to support the adhesion of HEK293 HEK cells when the cells are added to mouse SPP1 coated plates. The ED50 range is ≤ 1.5 ug/ml.

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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction. Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSLPVKVTD SGSSEEKLYS LHPDPIATWL VPDPSQKQNL LAPQNAVSSE EKDDFKQETL PSNSNESHDH MDDDDDDDDD DGDHAESEDS VDSDESDESH HSDESDETVT ASTQADTFTP IVPTVDVPNG RGDSLAYGLR SKSRSFQVSD EQYPDATDED LTSHMKSGES KESLDVIPVA QLLSMPSDQD NNGKGSHESS QLDEPSLETH RLEHSKESQE SADQSDVIDS QASSKASLEH QSHKFHSHKD KLVLDPKSKE DDRYLKFRIS HELESSSSEV NHHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interferon-alpha 14 Human Recombinant

Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.

Product # :

CYT-135

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source
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SDS-PAGE
Citations

Description

IFNA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a.) and having a molecular mass of 22.4kDa.IFNA14 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNA14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interferon alpha-14 (IFNA14) is a member of the alpha/beta interferon family. IFNA14 is produced by macrophages (IFN-alpha have antiviral activities). The interferon stimulates the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.
Background
What is the molecular weight/Mw of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein has a total Mw of 22.4kDa.

What is the source or expression system of IFNA14 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA14 HUMAN Protein?
The biological functionality of IFNA14 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNA14 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.

What applications can IFNA14 HUMAN Protein be used in?
IFNA14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA14 HUMAN Protein?
The endotoxin level is minimal, IFNA14 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin 12 Receptor Beta 1 Human Recombinant, Sf9

Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.

Product # :

CYT-894

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Description

IL12RB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-545 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 528 amino acids and having a molecular mass of 58.4kDa.IL12RB1 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL12RB1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol, 1mM EDTA and 0.1mM PMSF.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH
Background
What is the molecular weight/Mw of IL12RB1 HUMAN, SF9 Protein?
IL12RB1 HUMAN, SF9 Protein has a total Mw of 58.4kDa.

What is the source or expression system of IL12RB1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL12RB1 HUMAN, SF9 Protein?
IL12RB1 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12RB1 HUMAN, SF9 Protein?
The biological functionality of IL12RB1 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL12RB1 HUMAN, SF9 Protein?
CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH
What applications can IL12RB1 HUMAN, SF9 Protein be used in?
IL12RB1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12RB1 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL12RB1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12RB1 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL12RB1 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Lymphotoxin Beta Receptor Human Recombinant

Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

Product # :

CYT-853

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Description

LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.
Synonyms
Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic protein-2, Mouse Anti-Human

BMP-2, BMP2A.

Product # :

ANT-183

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Source

The BMP-2 antibody was prepared by affinity chromatography from ascites of BALB/c mouseinoculated by a hybridoma cell that secreted anti- BMP-2 monoclonal antibodies.

Formulation

Samples are lyophilized in sterile PBS buffers.

Purity

Greater than 90%, analysed by reducing SDS-PAGE.

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Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
Synonyms
BMP-2, BMP2A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
For long-term storage, keep aliquot samples at -70°C. Once reconstituted, samples are stable at 4°C for several weeks.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Applications
Applied in detections of antigen or antibody: ELISA or Western blot. For indirect ELISA, dilute antibody solution by 1: 250.
Type
Mouse Anti Human Monoclonal.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin-Like Growth Factor-1, Mouse Anti-Human

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

ANT-062

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human Growth Hormone
Ig Subclass
Mouse IgM
Clone
NYRhIGF1
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Boric acid precipitation

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Inositol Monophosphatase Domain Containing 1 Mouse Recombinant

Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3 Myo-inositol monophosphatase A3, Impad1, Impa3.

Product # :

PRO-2314

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Description

IMPAD1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356aa) and having a molecular mass of 36.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9 Insect cells.

Formulation

IMPAD1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.
Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3 Myo-inositol monophosphatase A3, Impad1, Impa3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Sonic HedgeHog Rat Recombinant

SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

Product # :

CYT-1099

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Description

Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Uteroglobin Rat Recombinant

Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

Product # :

CYT-820

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Shipped at Room temp

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biological activity
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Description

SCGB1A1 Rat Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 77 amino acids and having a molecular mass of 17.0kDa.

Source

Escherichia Coli.

Formulation

SCGB1A1 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0 ?g/ml, corresponding to a specific activity of >200IU/mg.

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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SCGB1A1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SCGB1A1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SSDICPGFLQ VLEALLLGSE SNYEAALKPF NPASDLQNAG TQLKRLVDTL PQETRINIVK LTEKILTSPL CEQDLRV

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vitamin D3, Mouse Anti Human

Product # :

ANT-780

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Description

Monoclonal antibody to Vitamin D3.

Formulation

PBS, sodium chloride and 0.095 % NaN3 as a preservative.

Purity

Protein is >95% pure.

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Introduction
Vitamin D3, also known as cholecalciferol, is a fat-soluble vitamin which takes a great part in maintaining bone health, immune function, and muscle strength. It is often called the sun vitamin as our body produces it naturally when our skin is exposed to UVB rays from sunlight.
Physical Appearance
Sterile filtered colorless solution.
Stability
Vitamin-D3 Antibody although stable at 4°C for 1 week, should be stored below -18°C.
Please prevent freeze thaw cycles.
Applications
Immunoassay.
Type
Mouse antibody Monoclonal.
Purification Method
Purified monoclonal IgG1 by protein A chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-2 Receptor alpha Human Recombinant, sf9

Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

Product # :

CYT-1020

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Description

IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.
Synonyms
Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
Background
What is the molecular weight/Mw of CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein has a total Mw of 52.1kDa.

What is the source or expression system of CD25 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD25 HUMAN, SF9 Protein?
The biological functionality of CD25 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CD25 HUMAN, SF9 Protein?
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

What applications can CD25 HUMAN, SF9 Protein be used in?
CD25 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD25 HUMAN, SF9 Protein?
The endotoxin level is minimal, CD25 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CD25 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CD25 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CD30 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.

Product # :

CYT-824

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Description

TNFSF8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (63-234 a.a.) and having a molecular mass of 22kDa.TNFSF8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFSF8 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
Synonyms
Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSD.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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