Search: 1000 results found for "basic transcription factor"

Description:

Leptin Ovine Recombinant, MTS tag

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-531

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Description

Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Ovine MTS tagged although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Leu-Leu-Pro.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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:

Allograft Inflammatory Factor 1 Like Human Recombinant

Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.

Product # :

CYT-007

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Description

AIF1L produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150a.a.) and having a molecular mass of 19.2kDa.AIF1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIF1L protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Synonyms
Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.
Background
Allograft Inflammatory Factor 1-Like Human Recombinant: Investigating its Role in Immune Responses and Potential Therapeutic Applications
1. Abstract
This paper seeks to provide an in-depth overview of Allograft Inflammatory Factor 1-Like Human Recombinant (AIF-1L), a significant protein involved in the regulation of inflammatory responses. By delving into the structure, biological functions, and pathological implications of AIF-1L, we attempt to shed light on its potential as a therapeutic target in immune-mediated disorders.
2. Introduction
AIF-1L belongs to the allograft inflammatory factor protein family and is implicated in immune responses. With its intricate interaction with a multitude of immune cells and involvement in various inflammatory and immune-related diseases, it serves as a pivotal point of interest for therapeutic intervention research.
3. Structure and Signaling of AIF-1L
AIF-1L shares a conserved EF-hand calcium-binding motif with its counterpart AIF-1, suggesting similar calcium-dependent activities. While its signaling pathway remains largely elusive, the protein is believed to modulate macrophage activation, an integral part of immune response regulation.
4. Biological Functions of AIF-1L
AIF-1L is fundamentally involved in immune response modulation, especially in the context of macrophage activation. It plays key roles in managing inflammation, cell proliferation, survival, and differentiation.
5. AIF-1L in Disease Pathology
AIF-1L is linked with a range of inflammatory and immune-related disorders, including but not limited to rheumatoid arthritis, atherosclerosis, and certain cancers. This association underscores its profound physiological relevance and potential as a therapeutic target.
6. Therapeutic Potential of AIF-1L
Given its central role in immune responses, AIF-1L presents a promising target for therapeutic strategies. Manipulating AIF-1L activity could pave the way for novel treatments of various inflammatory and immune-mediated diseases.
7. Conclusion and Future Perspectives
Though our comprehension of AIF-1L has made significant strides, there is still much terrain left to explore. Future research directed at the precise molecular mechanisms and pathological roles of AIF-1L will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1L Protein?
AIF1L Protein has a total Mw of 19.2kDa.

What is the source or expression system of AIF1L Protein?
Escherichia Coli.

What is the Purity of AIF1L Protein?
AIF1L Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1L Protein?
The biological functionality of AIF1L Protein will be determined in the future.

What is the amino acid sequence of AIF1L Protein?
MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.

What applications can AIF1L Protein be used in?
AIF1L Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1L Protein?
The endotoxin level is minimal, AIF1L 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:

Mitochondrial Ribosome Recycling Factor, Mouse Anti Human

MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

Product # :

ANT-098

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.

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Introduction
Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.
Synonyms
MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.
Physical Appearance
Sterile Filtered colorless solution.
Immunogen
Anti-human MRRF mAb, clone PAT7D10A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MRRF protein 56-262 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
Clone
PAT7D10A.
Applications
The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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
MRRF antibody was purified from mouse ascitic fluids by protein-G 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:

Heregulin-B2 Human Recombinant

Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.

Product # :

CYT-407

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Description

Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 10⁵ U/mg.

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Introduction
Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.
Synonyms
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin 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 NRG1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQ.

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:

Inhibitor of DNA Binding 1 Human Recombinant

bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.

Product # :

PRO-1426

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Description

ID1 Human Recombinant produced in E. coli is a single polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 18.5kDa. ID1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ID1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein which can form heterodimers with members of the basic HLH family of transcription factors. ID1 is lacking DNA binding activity and thus can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. ID1 participates in cell growth, senescence, and differentiation.
Synonyms
bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.
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 MGSMKVASGS TATAAAGPSC ALKAGKTASG AGEVVRCLSE QSVAISRCAG GAGARLPALL DEQQVNVLLY DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT PGGRGLPVRA PLSTLNGEIS ALTAEAACVP ADDRILCR.

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 Human Recombinant, Sf9

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

Product # :

CYT-417

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Description

Interleukin-3 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 CSF is fused to a C-terminal His-tag (6x His) and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.5X PBS pH-7.4.

Purity

Greater than 95.0% 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 TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/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 Interleukin-3 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.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 Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.
Background
What is the molecular weight/Mw of IL3 HUMAN, SF9 Protein?
IL3 HUMAN, SF9 Protein has a total Mw of 15kDa.

What is the source or expression system of IL3 HUMAN, SF9 Protein?
Insect Cells.
What is the Purity of IL3 HUMAN, SF9 Protein?
IL3 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 HUMAN, SF9 Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of IL3 HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.

What applications can IL3 HUMAN, SF9 Protein be used in?
IL3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL3 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 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 IL3 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:

Killer Cell Immunoglobulin-Like Receptor, 2 Domains Long Cytoplasmic Tail 3 Human Recombinant

Killer cell immunoglobulin-like receptor 2DL3, MHC class I NK cell receptor, Natural killer-associated transcript 2, NKAT-2, NKAT2a, NKAT2b, p58 natural killer cell receptor clone CL-6, p58 NK receptor, p58.2 MHC class-I-specific NK receptor, Killer inhibitory receptor cl 2-3, KIR-023GB, CD158 antigen-like family member B2, CD158b2 antigen, KIR2DL3, CD158B2, KIRCL23, NKAT2, p58, NKAT, GL183, CD158b, KIR-K7b, KIR-K7c, MGC129943.

Product # :

PRO-429

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Description

Recombinant KIR2DL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 23-223 and having a molecular mass of 22.2kDa.The KIR2DL3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 25mM Tris-HCl (pH-7.5).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DL3 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, cl-6, NKAT2 or KIR-K7), which recognizes class I MHC molecules (HLA-Cw1, -Cw3, -Cw7, and Cw8). KIR2DL3 inhibits the activity of NK cells thus preventing cell lysis.
Synonyms
Killer cell immunoglobulin-like receptor 2DL3, MHC class I NK cell receptor, Natural killer-associated transcript 2, NKAT-2, NKAT2a, NKAT2b, p58 natural killer cell receptor clone CL-6, p58 NK receptor, p58.2 MHC class-I-specific NK receptor, Killer inhibitory receptor cl 2-3, KIR-023GB, CD158 antigen-like family member B2, CD158b2 antigen, KIR2DL3, CD158B2, KIRCL23, NKAT2, p58, NKAT, GL183, CD158b, KIR-K7b, KIR-K7c, MGC129943.
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
MEGVHRKPSL LAHPGPLVKS EETVILQCWS DVRFQHFLLH REGKFKDTLH LIGEHHDGIS KANFSIGPMM QDLAGTYRCY GSVTHSPYQL SAPSDPLDIV ITGLYEKPSL SAQPGPTVLA GESVTLSCSS RSSYDMYHLS REGEAHERRF SAGPKVNGTF QADFPLGPAT HGGTYRCFGS FRDSPYEWSN SSDPLLVSVT GN.

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-16 Human Recombinant, (130 a.a.)

IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

Product # :

CYT-536

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Description

Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 13.5 kDa. The IL-16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-16 was lyophilized at 1 mg/ml in 10mM NaP, pH-7.5.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to chemoattract human CD4+ T lymphocytes using a concentration range of 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL16 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 Interleukin-16 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Asp-Leu-Asn.

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:

Vascular Endothelial Growth Factor Receptor-2 Human Recombinant

KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.

Product # :

PKA-242

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Description

Soluble VEGFR-2 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide having a molecular mass of 116 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.The sKDR is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

KDR was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM MES pH-5.5 and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGFR-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLK1 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 VEGFR2 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ASVGLPSVSLD LPRLSIQKDI LTIKANTTLQ ITCRGQRDLD WLWPNNQSGS EQRVEVTECS DGLFCKTLTI PKVIGNDTGA YKCFYRETDL ASVIYVYVQD YRSPFIASVS DQHGVVYITE NKNKTVVIPC LGSISNLNVS LCARYPEKRF VPDGNRISWD SKKGFTIPSY MISYAGMVFC EAKINDESYQ SIMYIVVVVG YRIYDVVLSP SHGIELSVGE KLVLNCTART ELNVGIDFNW EYPSSKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDGVTRS DQGLYTCAAS SGLMTKKNST FVRVHEKPFV AFGSGMESLV EATVGERVRI PAKYLGYPPP EIKWYKNGIP LESNHTIKAG HVLTIMEVSE RDTGNYTVIL TNPISKEKQS HVVSLVVYVP PQIGEKSLIS PVDSYQYGTT QTLTCTVYAI PPPHHIHWYW QLEEECANEP SQAVSVTNPY PCEEWRSVED FQGGNKIEVN KNQFALIEGK NKTVSTLVIQ AANVSALYKC EAVNKVGRGE RVISFHVTRG PEITLQPDMQ PTEQESVSLW CTADRSTFEN LTWYKLGPQP LPIHVGELPT PVCKNLDTLW KLNATMFSNS TNDILIMELK NASLQDQGDY VCLAQDRKTK KRHCVVRQLT VLERVAPTIT GNLENQTTSI GESIEVSCTA SGNPPPQIMW FKDNETLVED SGIVLKDGNR NLTIRRVRKE DEGLYTCQAC SVLGCAKVEA FFIIEGA.

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:

SERTA Domain Containing 2 Human Recombinant

SERTA domain-containing protein 2, Transcriptional regulator interacting with the PHD-bromodomain 2, TRIP-Br2, SERTAD2, KIAA0127, SERTA domain containing 2, Sei-2.

Product # :

PRO-2021

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Description

SERTAD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.3 kDa.SERTAD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SERTAD2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SERTA domain containing 2 (SERTAD2) takes part at E2F-responsive promoters to integrate signals which are given by PHD- and bromodomain-containing transcription factors. The SERTAD2 protein is taking part in modulating fat storage by down-regulating the expression of key genes which take part in thermogenesis, adipocyte lipolysis and oxidative metabolism.
Synonyms
SERTA domain-containing protein 2, Transcriptional regulator interacting with the PHD-bromodomain 2, TRIP-Br2, SERTAD2, KIAA0127, SERTA domain containing 2, Sei-2.
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 MGSMLGKGGK RKFDEHEDGL EGKIVSPCDG PSKVSYTLQR QTIFNISLMK LYNHRPLTEP SLQKTVLINN MLRRIQEELK QEGSLRPMFT PSSQPTTEPS DSYREAPPAF SHLASPSSHP CDLGSTTPLE ACLTPASLLE DDDDTFCTSQ AMQPTAPTKL SPPALLPEKD SFSSALDEIE ELCPTSTSTE AATAATDSVK GTSSEAGTQK LDGPQESRAD DSKLMDSLPG NFEITTSTGF LTDLTLDDIL FADIDTSMYD FDPCTSSSGT ASKMAPVSAD DLLKTLAPYS SQPVTPSQPF KMDLTELDHI MEVLVGS.

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-33 Mouse Recombinant

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

Product # :

CYT-655

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Description

Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

Source

Escherichia Coli.

Formulation

The Mouse IL-33 was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of murine D10S cells is 0.04ng/ml, corresponding to a specific activity of 2.5x10⁷units/mg.

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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-33 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI.

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-7 Human Recombinant, HEK

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-197

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Description

IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The IL7 was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
Background
What is the molecular weight/Mw of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein has a total Mw of 24.5kDa.

What is the source or expression system of IL7 HUMAN, HEK Protein?
HEK.
What is the Purity of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN, HEK Protein?
The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

What applications can IL7 HUMAN, HEK Protein be used in?
IL7 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7 HUMAN, HEK Protein?
The endotoxin level is minimal, IL7 HUMAN, HEK Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7 HUMAN, HEK 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 IL7 HUMAN, HEK?
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-1 beta Human Recombinant

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

CYT-208

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Shipped at Room temp

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Description

Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.

Purity

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

Biological Activity

The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

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Introduction
Interleukin-1b is produced by activated macrophages, IL-1 Beta stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B 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
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 Beta 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 Interleukin-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.
Background
What is the molecular weight/Mw of IL1B HUMAN Protein?
IL1B HUMAN Protein has a total Mw of 17kDa.

What is the source or expression system of IL1B HUMAN Protein?
Escherichia Coli.

What is the Purity of IL1B HUMAN Protein?
IL1B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B HUMAN Protein?
The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

What is the amino acid sequence of IL1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.

What applications can IL1B HUMAN Protein be used in?
IL1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B HUMAN Protein?
The endotoxin level is minimal, IL1B 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 0.631 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 calibrated solution of IL-1 beta Recombinant 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-1 beta Rhesus Macaque Recombinant

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

CYT-718

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Description

Interleukin-1 beta Monkey Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17.3 kDa. The IL-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with 1x PBS pH-7.4

Purity

Greater than 98.0% 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 D10.G4.1 mouse helper T cells is typically 3-10pg/mL.

More Info

Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B 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
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1B 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 IL1B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APVRSLHCTL RDAQLKSLVM SGPYELKALH LQGQDLEQQV VFSMSFVQGE ESNDKIPVAL GLKAKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTRGG QDITDFTMQF VSS.
Background
What is the molecular weight/Mw of IL1B MONKEY Protein?
IL1B MONKEY Protein has a total Mw of 17.3kDa.

What is the source or expression system of IL1B MONKEY Protein?
Escherichia Coli.

What is the Purity of IL1B MONKEY Protein?
IL1B MONKEY Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B MONKEY Protein?
The ED50 as determined by the dose-dependant stimulation of D10.G4.1 mouse helper T cells is typically 3-10pg/mL.

What is the amino acid sequence of IL1B MONKEY Protein?
APVRSLHCTL RDAQLKSLVM SGPYELKALH LQGQDLEQQV VFSMSFVQGE ESNDKIPVAL GLKAKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTRGG QDITDFTMQF VSS.

What applications can IL1B MONKEY Protein be used in?
IL1B MONKEY Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B MONKEY Protein?
The endotoxin level is minimal, IL1B MONKEY 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:

APEX Nuclease-1 Human Recombinant

APEX nuclease (multifunctional DNA repair enzyme) 1, APE, REF1, HAP1, APX, APEN, APEX, Apurinic-apyrimidinic endonuclease 1, Protein REF-1, AP endonuclease 1, APEX nuclease (multifunctional DNA repair enzyme), APE-1, deoxyribonuclease (apurinic or apyrimidinic), apurinic/apyrimidinic exonuclease, AP endonuclease class I, multifunctional DNA repair enzyme, redox factor 1, EC 4.2.99.18.

Product # :

ENZ-059

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Description

APEX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 332 amino acids (1-318a.a.) and having a molecular mass of 36.9kDa.APEX1 protein is fused to a 14 amino acid T7-tag at N-terminus and is purified by standard chromatography.

Source

Escherichia Coli.

Formulation

APEX1 Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 0.2M NaCl, and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
APEX1 is in charge of the incision of DNA basic sites during base excision repair. APEX1 also stimulates the DNA binding activity of numerous transcription factors which take part in cancer promotion and progression. APEX1 is part of the cellular response to oxidative stress and protects cells from the genotoxic and cytotoxic effect of oxidizing agents.
Synonyms
APEX nuclease (multifunctional DNA repair enzyme) 1, APE, REF1, HAP1, APX, APEN, APEX, Apurinic-apyrimidinic endonuclease 1, Protein REF-1, AP endonuclease 1, APEX nuclease (multifunctional DNA repair enzyme), APE-1, deoxyribonuclease (apurinic or apyrimidinic), apurinic/apyrimidinic exonuclease, AP endonuclease class I, multifunctional DNA repair enzyme, redox factor 1, EC 4.2.99.18.
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.Please avoid freeze thaw cycles.
Amino Acid Sequence
MASMTGGQQM GRGSMPKRGK KGAVAEDGDE LRTEPEAKKS KTAAKKNDKE AAGEGPALYE DPPDQKTSPS GKPATLKICS WNVDGLRAWI KKKGLDWVKE EAPDILCLQE TKCSENKLPA ELQELPGLSH QYWSAPSDKE GYSGVGLLSR QCPLKVSYGI GEEEHDQEGR VIVAEFDSFV LVTAYVPNAG RGLVRLEYRQ RWDEAFRKFL KGLASRKPLV LCGDLNVAHE EIDLRNPKGN KKNAGFTPQE RQGFGELLQA VPLADSFRHL YPNTPYAYTF WTYMMNARSK NVGWRLDYFL LSHSLLPALC DSKIRSKALG SDHCPITLYL AL.

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:

Fibroblast Growth Factor Receptor-3 Human Recombinant, His Tag

CD333 Antigen, HSFGFR3EX, EC 2.7.10, CD333, CEK2, ACH, Fibroblast Growth Factor Receptor 3, EC 2.7.10.1, FGFR-3, JTK4, Fibroblast Growth Factor Receptor 3 Variant 4, Achondroplasia, Thanatophoric Dwarfism, Hydroxyaryl-Protein Kinase, Tyrosine Kinase JTK4.

Product # :

PKA-101

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Description

FGFR3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 592 amino acids (23-375a.a.) and having a molecular mass of 65.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). FGFR3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGFR3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
Synonyms
CD333 Antigen, HSFGFR3EX, EC 2.7.10, CD333, CEK2, ACH, Fibroblast Growth Factor Receptor 3, EC 2.7.10.1, FGFR-3, JTK4, Fibroblast Growth Factor Receptor 3 Variant 4, Achondroplasia, Thanatophoric Dwarfism, Hydroxyaryl-Protein Kinase, Tyrosine Kinase JTK4.
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
ESLGTEQRVV GRAAEVPGPE PGQQEQLVFG SGDAVELSCP PPGGGPMGPT VWVKDGTGLV PSERVLVGPQ RLQVLNASHE DSGAYSCRQR LTQRVLCHFS VRVTDAPSSG DDEDGEDEAE DTGVDTGAPY WTRPERMDKK LLAVPAANTV RFRCPAAGNP TPSISWLKNG REFRGEHRIG GIKLRHQQWS LVMESVVPSD RGNYTCVVEN KFGSIRQTYT LDVLERSPHR PILQAGLPAN QTAVLGSDVE FHCKVYSDAQ PHIQWLKHVE VNGSKVGPDG TPYVTVLKTA GANTTDKELE VLSLHNVTFE DAGEYTCLAG NSIGFSHHSA WLVVLPAEEE LVEADEAGSV YAGLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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:

Interleukin-1 alpha Human Recombinant, His Tag

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-479

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Quantity :

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Description

IL-1A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids fragment (113-271) with an amino-terminal hexahistidine tag and having a total molecular mass of 22.5kDa. The Interleukin-1 alpha His-tag is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1 alpha His-tag protein is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced by inflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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 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.
Background
What is the molecular weight/Mw of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein has a total Mw of 22.5kDa.

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

What is the Purity of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN, HIS Protein?
The biological functionality of IL1A HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein is composed from 159 amino acids.

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

What is the endotoxin level for IL1A HUMAN, HIS Protein?
The endotoxin level is minimal, IL1A 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:

Interleukin-9 Human Recombinant, Sf9

Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.

Product # :

CYT-866

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Description

IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL-9 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL-9 is a factor which is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
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
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein has a total Mw of 23kDa.

What is the source or expression system of IL9 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 Protein?
The biological functionality of IL9 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL9 HUMAN, SF9 Protein?
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.

What applications can IL9 HUMAN, SF9 Protein be used in?
IL9 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 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 IL9 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:

Vascular Endothelial Growth Factor Human Recombinant, His

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-496

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Description

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain (aa 207-371) containing a total of 185 amino acids and having a molecular mass of 21.3 kDa (corresponding to Isoform L-VEGF165 UniProt acc#P15692-11). The VEGF is fused to a 20 a.a His-tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VEGF His (0.5mg/ml) is supplied in 20mM Tris-HCl pH-8.5, 50% glycerol, 5mM DTT, 200mM NaCl & 2mM EDTA.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

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-22 Mouse Recombinant, Pegylated

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-701

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Shipped at Room temp

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Description

Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

Purity

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

Biological Activity

The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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-5 Rat Recombinant

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

Product # :

CYT-387

Price :

Quantity :

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Shipped at Room temp

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Description

Interleukin-5 Rat Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 13074 Dalton.The IL-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ range=0.3-1.0 ng/ml as determined by the dose-dependant stimulation of the proliferation of BCL-1 cells.

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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-5 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleikin-5 Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Ile-Pro-Met.
Background
What is the molecular weight/Mw of IL 5 RAT Protein?
IL 5 RAT Protein has a total Mw of 13kDa.

What is the source or expression system of IL 5 RAT Protein?
Escherichia Coli.

What is the Purity of IL 5 RAT Protein?
IL 5 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 RAT Protein?
The ED50 range=0.3-1.0 ng/ml as determined by the dose-dependant stimulation of the proliferation of BCL-1 cells.

What is the amino acid sequence of IL 5 RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Ile-Pro-Met.

What applications can IL 5 RAT Protein be used in?
IL 5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 RAT Protein?
The endotoxin level is minimal, IL 5 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 RAT 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 5 RAT?
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:

SH2 domain containing 1B Human Recombinant

SH2 Domain Containing 1B, EWS/FLI1-Activated Transcript 2, EAT-2, EAT2, SH2 Domain-Containing Molecule EAT2, SH2 Domain-Containing Protein 1B, SH2 domain-containing protein 1B, EWS/FLI1-activated transcript 2, EAT-2.

Product # :

PRO-2470

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Shipped with Ice Packs

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Description

SH2D1B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 141 amino acids (1-132a.a.) and having a molecular mass of 16.4kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SH2D1B is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SH2D1B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SH2 domain-containing protein 1B, also known as SH2D1B activates NK cells. SH2D1B participates in controlling signal transduction through at least 4 receptors, CD84, SLAMF1, LY9 and CD244, expressed on the surface of professional antigen-presenting cells. Two isoforms of the human SH2D1B are produced by alternative splicing. Superior Mesenteric Artery Syndrome is one of the diseases which is associated with SH2D1B.
Synonyms
SH2 Domain Containing 1B, EWS/FLI1-Activated Transcript 2, EAT-2, EAT2, SH2 Domain-Containing Molecule EAT2, SH2 Domain-Containing Protein 1B, SH2 domain-containing protein 1B, EWS/FLI1-activated transcript 2, EAT-2.
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
ADPMDLPYYH GRLTKQDCET LLLKEGVDGN FLLRDSESIP GVLCLCVSFK NIVYTYRIFR EKHGYYRIQT AEGSPKQVFP SLKELISKFE KPNQGMVVHL LKPIKRTSPS LRWRGLKLEL ETFVNSNSDY VDVLPHHHHH H.

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-6 Rhesus Macaque Recombinant

IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

Product # :

CYT-174

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL 6 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 186 amino acids and having a molecular mass of 21.1kDa.The IL 6 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 and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED50 determined by a cell proliferation assay using IL-6-dependent murine 7TD1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.

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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-6 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 IL-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPVLPGEDS KNVAAPHSQP LTSSERIDKH IRYILDGISA LRKETCNRSN MCESSKEALA ENNLNLPKMA EKDGCFQSGF NEDTCLVKII TGLLEFEVYL EYLQNRFESS EEQARAVQMS TKVLIQFLQK KAKNLDAITT PEPTTNASLL TKLQAQNQWL QDMTTHLILR SFKEFLQSNL RALRQM
Background
Research Paper on Interleukin-6 Rhesus Macaque Recombinant
Abstract:
Interleukin-6 (IL-6) Rhesus Macaque Recombinant holds a significant role in the realm of immunological exploration. This research paper delves into the molecular intricacies and implications of IL-6 Rhesus Macaque Recombinant in immune modulation. Through an investigation of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its contribution to understanding immune responses.
Introduction:
IL-6 Rhesus Macaque Recombinant is a key player in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.
Molecular Structure and Insights:
Examining the molecular composition of IL-6 Rhesus Macaque Recombinant, we uncover its role in immune signaling. Its interactions and functions contribute to the fine-tuning of immune responses.
Exploring Immune Dynamics:
IL-6's influence on immune cell activation and inflammation is well-acknowledged. IL-6 Rhesus Macaque Recombinant provides a tool to delve deeper into these immune processes, enriching our comprehension of cytokine-mediated functions.
Synonyms and Network Connections:
Understanding IL-6's synonyms, such as DIF, TNFA, and TNFSF2, adds depth to our understanding of immune signaling networks. IL-6 Rhesus Macaque Recombinant helps uncover the complexity of these interconnected pathways.
Potential Applications in Research and Beyond:
Beyond research settings, IL-6 Rhesus Macaque Recombinant holds potential in deciphering immune-related diseases. Its significance extends to possible therapeutic interventions and diagnostic applications.
Clinical Implications and Future Prospects:
The clinical relevance of IL-6 Rhesus Macaque Recombinant is underlined by its role in diseases characterized by altered IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies in disease management.
Conclusion:
In the realm of immunology, IL-6 Rhesus Macaque Recombinant stands as a pivotal tool. Its molecular insights, pivotal functions, and potential implications position it as a valuable asset for advancing our understanding of immune regulation.
What is the molecular weight/Mw of IL6 RHESUS MACAQUE Protein?
IL6 RHESUS MACAQUE Protein has a total Mw of 21.1kDa.

What is the source or expression system of IL6 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL6 RHESUS MACAQUE Protein?
IL6 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 RHESUS MACAQUE Protein?
Fully biologically active when compared to standard. The ED50 determined by a cell proliferation assay using IL-6-dependent murine 7TD1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.

What is the amino acid sequence of IL6 RHESUS MACAQUE Protein?
MAPVLPGEDS KNVAAPHSQP LTSSERIDKH IRYILDGISA LRKETCNRSN MCESSKEALA ENNLNLPKMA EKDGCFQSGF NEDTCLVKII TGLLEFEVYL EYLQNRFESS EEQARAVQMS TKVLIQFLQK KAKNLDAITT PEPTTNASLL TKLQAQNQWL QDMTTHLILR SFKEFLQSNL RALRQM.
What applications can IL6 RHESUS MACAQUE Protein be used in?
IL6 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL6 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6 RHESUS MACAQUE 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 IL6 RHESUS MACAQUE?
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-5 Human Recombinant, Sf9

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

Product # :

CYT-999

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-134a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).IL5 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL5 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.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED₅₀ for this effect is less or equal to 1.5 ng/ml.

More Info

Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
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
ADPIPTEIPT SALVKETLAL LSTHRTLLIA NETLRIPVPV HKNHQLCTEE IFQGIGTLES QTVQGGTVER LFKNLSLIKK YIDGQKKKCG EERRRVNQFL DYLQEFLGVM NTEWIIESHH HHHH.
Background
What is the molecular weight/Mw of IL 5 HUMAN, SF9 Protein?
IL 5 HUMAN, SF9 Protein has a total Mw of 14.2kDa.

What is the source or expression system of IL 5 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 HUMAN, SF9 Protein?
IL 5 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 HUMAN, SF9 Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effect is less or equal to 1.5 ng/ml.

What is the amino acid sequence of IL 5 HUMAN, SF9 Protein?
ADPIPTEIPT SALVKETLAL LSTHRTLLIA NETLRIPVPV HKNHQLCTEE IFQGIGTLES QTVQGGTVER LFKNLSLIKK YIDGQKKKCG EERRRVNQFL DYLQEFLGVM NTEWIIESHH HHHH.

What applications can IL 5 HUMAN, SF9 Protein be used in?
IL 5 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL 5 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 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 IL 5 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.

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