Search: 1000 results found for "fc fragment of igg receptor"

Description:

Transmembrane And Immunoglobulin Domain Containing 2 Human Recombinant

IGPR-1, IGPR1,TMIGD2, Transmembrane and immunoglobulin domain-containing protein 2 isoform1, CD28 homolog, CD28H, Immunoglobulin and proline-rich receptor 1.

Product # :

PRO-2808

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Description

TMIGD2 Human Recombinant is a single, glycosylated, polypeptide chain (23-150 a.a) containing a total of 361 amino acids and having a molecular mass of 40.1 kDa. TMIGD2 is fused to a 233 a.a hIgG -Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The TMIGD2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤ 200 ng/ml and is measured by its binding ability in a functional ELISA with Human HHLA2.

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Synonyms
IGPR-1, IGPR1,TMIGD2, Transmembrane and immunoglobulin domain-containing protein 2 isoform1, CD28 homolog, CD28H, Immunoglobulin and proline-rich receptor 1.
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
LSVQQGPNLL QVRQGSQATL VCQVDQATAW ERLRVKWTKD GAILCQPYIT NGSLSLGVCG PQGRLSWQAP SHLTLQLDPV SLNHSGAYVC WAAVEIPELE EAEGNITRLF VDPDDPTQNR NRIASFPGLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPGK.
Background
TMIGD2 in Autoimmune Disorders:
Conversely, dysregulation of TMIGD2 may contribute to autoimmune disorders, where the immune system mistakenly targets the body's own tissues. Investigations into TMIGD2 Human Recombinant may shed light on its role in immune tolerance and the prevention of excessive immune reactions. Deciphering the nuances of TMIGD2's functions provides potential insights for therapeutic interventions in autoimmune conditions.
Challenges and Future Directions:
While the potential of TMIGD2 Human Recombinant in immune modulation is promising, challenges persist. Fine-tuning its applications, understanding its interactions with various immune cell types, and deciphering the context-dependent nature of its functions are critical considerations for translational success. Additionally, exploring the potential dual role of TMIGD2 in cancer immunity and autoimmune disorders poses a challenge in the pursuit of targeted therapeutic strategies.
TMIGD2 Human Recombinant emerges as a promising protagonist in the narrative of immune modulation, offering a controlled platform for scientific exploration. Its structural insights, cellular functions, and implications in immune regulation position it as a key player in the evolving landscape of immunotherapy and immune-related disorders. As researchers continue to unravel the molecular intricacies of TMIGD2, they not only deepen our understanding of immune responses but also pave the way for transformative advancements in cancer immunotherapy and autoimmune disease therapeutics, shaping the future of precision medicine and immunomodulatory interventions.

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:

GDNF Family Receptor Alpha 1 Human Recombinant

GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

Product # :

CYT-1026

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Description

GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).

Source

HEK293 cells.

Formulation

GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
Synonyms
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
Background
What is the molecular weight/Mw of GFRA1 Protein?
GFRA1 Protein has a total Mw of 46kDa.

What is the source or expression system of GFRA1 Protein?
HEK293 cells.
What is the Purity of GFRA1 Protein?
GFRA1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA1 Protein?
The biological functionality of GFRA1 Protein will be determined in the future.

What is the amino acid sequence of GFRA1 Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

What applications can GFRA1 Protein be used in?
GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA1 Protein?
The endotoxin level is minimal, GFRA1 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:

Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-521

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Description

MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.

Source

Escherichia Coli.

Formulation

Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.

Purity

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

Biological Activity

Measured by its ability to bind rhCD74 in a functional ELISA.

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Physical Appearance
Sterile Filtered lyophilized powder.
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.

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:

IFN-Beta 1b Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.

Product # :

CYT-234

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Description

IFN beta 1b Human Recombinant produced in E.Coli is a single, non-glycosylated mutein (variant form) of human IFN beta-1b polypeptide chain containing 165 amino acids and having a molecular mass of 18510.86 Dalton.The IFN-beta gene was cloned from human fibroblasts and altered to substitute Serine for the Cysteine residue found at position 17. IFN beta-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 1mg/ml solution containing 50mg Human Albumin & 50mg dextrose.

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 a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 32 x 10⁶ IU/mg.

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Introduction
IFN-beta 1b has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-beta 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNB 1b 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 IFN beta-1b in sterile 18M-cm H2O at a concentration of 0.25mg/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 Ser-Tyr-Asn-Leu-Leu.
Background
What is the molecular weight/Mw of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein has a total Mw of 18.5kDa.

What is the source or expression system of IFN BETA 1B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1B HUMAN Protein?
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 32 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Tyr-Asn-Leu-Leu.

What applications can IFN BETA 1B HUMAN Protein be used in?
IFN BETA 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN BETA 1B HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1B 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 1.493 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 IFN-beta 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:

ERGIC And Golgi 3 Human Recombinant

ERGIC And Golgi 3,Serologically Defined Breast Cancer Antigen NY-BR-84, Serologically Defined Breast Cancer Antigen 84, C20orf47, SDBCAG84, Erv46, Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3, Endoplasmic Reticulum-Localized Protein ERp43,Chromosome 20 Open Reading Frame 47,DJ477O4.2, NY-BR-84, PRO0989,CGI-54, ERGIC3.

Product # :

PRO-2158

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Description

ERGIC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-341 a.a) and having a molecular mass of 36.1kDa.ERGIC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ERGIC3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ERGIC And Golgi 3, also known as ERGIC3 is a member of the ERGIC family and interacts with ERGIC1/ERGIC32. ERGIC3 takes part in the transport between endoplasmic reticulum and Golgi. One of the diseases which is associated with ERGIC3 is Breast Cancer.
Synonyms
ERGIC And Golgi 3,Serologically Defined Breast Cancer Antigen NY-BR-84, Serologically Defined Breast Cancer Antigen 84, C20orf47, SDBCAG84, Erv46, Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3, Endoplasmic Reticulum-Localized Protein ERp43,Chromosome 20 Open Reading Frame 47,DJ477O4.2, NY-BR-84, PRO0989,CGI-54, ERGIC3.
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 MGSQYYLTTE VHPELYVDKS RGDKLKINID VLFPHMPCAY LSIDAMDVAG EQQLDVEHNL FKQRLDKDGI PVSSEAERHE LGKVEVTVFD PDSLDPDRCE SCYGAEAEDI KCCNTCEDVR EAYRRRGWAF KNPDTIEQCR REGFSQKMQE QKNEGCQVYG FLEVNKVAGN FHFAPGKSFQ QSHVHVHDLQ SFGLDNINMT HYIQHLSFGE DYPGIVNPLD HTNVTAPQAS MMFQYFVKVV PTVYMKVDGE VLRTNQFSVT RHEKVANGLL GDQGLPGVFV LYELSPMMVK LTEKHRSF

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:

Fructosamine 3 Kinase Related Protein Human Recombinant

Ketosamine-3-kinase, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP, FN3KL.

Product # :

PKA-051

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Description

FN3KRP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.8kDa.FN3KRP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FN3KRP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ketosamine-3-kinase (FN3KRP) catalyzes the phosphorylation of psicosamines and ribulosamines compared to the adjacent gene which encodes a highly analogous enzyme, fructosamine-3-kinase that has different substrate specificity. The activity of both enzymes may cause deglycation of proteins to reinstate their function. A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). The proteins altered in this way, are less active or functional.
Synonyms
Ketosamine-3-kinase, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP, FN3KL.
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 MGSMEELLRR ELGCSSVRAT GHSGGGCISQ GRSYDTDQGR VFVKVNPKAE ARRMFEGEMA SLTAILKTNT VKVPKPIKVL DAPGGGSVLV MEHMDMRHLS SHAAKLGAQL ADLHLDNKKL GEMRLKEAGT VGRGGGQEER PFVARFGFDV VTCCGYLPQV
NDWQEDWVVF YARQRIQPQM DMVEKESGDR EALQLWSALQ LKIPDLFRDL EIIPALLHGD LWGGNVAEDS SGPVIFDPAS FYGHSEYELA IAGMFGGFSS SFYSAYHGKI PKAPGFEKRL QLYQLFHYLN HWNHFGSGYR GSSLNIMRNL VK.

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-3 Human Recombinant

Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

Product # :

PKA-244

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Description

Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

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Introduction
All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.
Synonyms
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/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:

TNF Ligand Receptor Superfamily Member 10B Human Recombinant, Sf9

TNFRSF10B, CD262, DR5, KILLER, KILLER/DR5, TRAIL-R2, TRAILR2, TRICK2, TRICK2A, TRICK2B, TRICKB, ZTNFR9, Death receptor 5, TNF-related apoptosis-inducing ligand receptor 2.

Product # :

CYT-1055

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Description

TNFRSF10B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 394 amino acids (56-210a.a.) and having a molecular mass of 43.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10B is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

TNFRSF10B protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect ≤ to 5ng/ml with TRAIL

.

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Introduction
TRAIL Receptor-1 (DR4) and TRAIL Receptor-2(DR5) are members of the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which is capable of activating the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L.
Synonyms
TNFRSF10B, CD262, DR5, KILLER, KILLER/DR5, TRAIL-R2, TRAILR2, TRICK2, TRICK2A, TRICK2B, TRICKB, ZTNFR9, Death receptor 5, TNF-related apoptosis-inducing ligand receptor 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
ITQQDLAPQQ RAAPQQKRSS PSEGLCPPGH HISEDGRDCI SCKYGQDYST HWNDLLFCLR CTRCDSGEVE LSPCTTTRNT VCQCEEGTFR EEDSPEMCRK CRTGCPRGMV KVGDCTPWSD IECVHKESGT KHSGEVPAVE ETVTSSPGTP ASPCSLEPKS 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:

Gliadin Alpha Wheat Recombinant

Product # :

PRO-2147

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Description

Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.

Purity

Protein is >90% pure.

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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
Physical Appearance
Sterile Filtered clear solution.
Stability
Gliadin Alpha although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.

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:

Erythropoietin-Alpha Fc-Chimera Human Recombinant

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Product # :

CYT-325

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Description

Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

Source

Chinese Hamster Ovary Cells(CHO).

Formulation

Each mg of lyophilized powder contains 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-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 10⁵ IU/mg.

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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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 Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 140kDa.

What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).

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

What is the Biological Activity of EPOETIN Protein?
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

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

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

Macrophage Migration Inhibitory Factor Rat Recombinant

Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

Product # :

CYT-193

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Description

MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

More Info

Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

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-17F Mouse Recombinant

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-642

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Description

IL17F Mouse Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 266 amino acids and having a molecular mass of 29.8 kDa. The Mouse IL-17F is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17F was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

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

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Murine IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17F 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 Mouse IL17F in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSP
WDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRR
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAA.

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-19 Human Recombinant, HEK

Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19

Product # :

CYT-1192

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Description

IL19 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-177) containing 164 amino acids and having a molecular mass of 19.1 kDa.IL19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

IL19 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. IL19 binds the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.
Synonyms
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19
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
DGSHMLRRCL ISTDMHHIEE SFQEIKRAIQ AKDTFPNVTI LSTLETLQII KPLDVCCVTK NLLAFYVDRV FKDHQEPNPK ILRKISSIAN SFLYMQKTLR QCQEQRQCHC RQEATNATRV IHDNYDQLEV HAAAIKSLGE LDVFLAWINK NHEVMFSAHH 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:

Fractalkine (CX3CL1) Human Recombinant, Sf9

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-042

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Description

Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

What applications can CX3CL1 HUMAN, SF9 Protein be used in?
CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CX3CL1 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 CX3CL1 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:

Platelet-Derived Growth Factor Receptor, Beta Human Recombinant

Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b AntigenNDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,Platelet-Derived Growth Factor Receptor Beta.

Product # :

CYT-1051

Price :

Quantity :

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Shipped with Ice Packs

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Description

PDGFRB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 739 amino acids (33-532a.a.) and having a molecular mass of 83.3kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).PDGFRB is expressed with an 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

PDGFRB protein solution (0.25mg/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
Platelet-derived growth factor receptor beta (PDGFRB), belongs to the class III subfamily of receptor tyrosine kinases (RTK) which also consist of the receptors for Flt3-ligand, SCF and M-CSF. PDGFRB takes a vital part in blood vessel development by promoting growth, migration as well as recruitment of pericytes and smooth muscle cells to endothelial cells. PDGFRB helps in rearrangement of the actin cytoskeleton in addition the formation of membrane ruffles. PDGFRB phosphorylates, NCK1, PIK3R1, PTPN11, CBL, SHC1, RASA1/GAP and PLCG1.
Synonyms
Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b Antigen
NDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,
Platelet-Derived Growth Factor Receptor Beta.
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
LVVTPPGPEL VLNVSSTFVL TCSGSAPVVW ERMSQEPPQE MAKAQDGTFS SVLTLTNLTG LDTGEYFCTH NDSRGLETDE RKRLYIFVPD PTVGFLPNDA EELFIFLTEI TEITIPCRVT DPQLVVTLHE KKGDVALPVP YDHQRGFSGI FEDRSYICKT TIGDREVDSD AYYVYRLQVS SINVSVNAVQ TVVRQGENIT LMCIVIGNEV VNFEWTYPRK ESGRLVEPVT DFLLDMPYHI RSILHIPSAE LEDSGTYTCN VTESVNDHQD EKAINITVVE SGYVRLLGEV GTLQFAELHR SRTLQVVFEA YPPPTVLWFK DNRTLGDSSA GEIALSTRNV SETRYVSELT LVRVKVAEAG HYTMRAFHED AEVQLSFQLQ INVPVRVLEL SESHPDSGEQ TVRCRGRGMP QPNIIWSACR DLKRCPRELP PTLLGNSSEE ESQLETNVTY WEEEQEFEVV STLRLQHVDR PLSVRCTLRN AVGQDTQEVI VVPHSLPFKV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

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:

Hepatocyte Growth Factor Receptor Mouse Recombinant

hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

Product # :

CYT-1139

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Quantity :

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Description

HGF Receptor Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 1146 amino acids (25-931aa) and having a molecular mass of 127.8kDa. HGF is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

HGF Receptor protein (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
HGF, also known as scatter factor (SF) and Hepatocyte growth factor, is secreted from mesenchymal cells, targets and acts mainly on epithelial and endothelial cells. The protein is a paracrine cellular growth, motility and morphogenic factor. HGF can also be part of haemopoietic progenitor cells and T cells. HGF has a crucial role in embryonic organ development, mainly in myogenesis. In adults HGF takes part in organ regeneration and wound healing.
Synonyms
hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.
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
ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
Background
What is the molecular weight/Mw of HGFR MOUSE Protein?
HGFR MOUSE Protein has a total Mw of 127.8kDa.

What is the source or expression system of HGFR MOUSE Protein?
Sf9, Baculovirus cells.

What is the Purity of HGFR MOUSE Protein?
HGFR MOUSE Protein is >85% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of HGFR MOUSE Protein?
ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
What applications can HGFR MOUSE Protein be used in?
HGFR MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein Human Recombinant

Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.

Product # :

PRO-1181

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Description

TIRAP Human Recombinant produced in E. coli is a single polypeptide chain containing 244 amino acids (1-221) and having a molecular mass of 26.3 kDa.TIRAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TIRAP solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.
Synonyms
Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
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 MGSMASSTSL PAPGSRPKKP LGKMADWFRQ TLLKKPKKRP NSPESTSSDA SQPTSQDSPL PPSLSSVTSP SLPPTHASDS GSSRWSKDYD VCVCHSEEDL VAAQDLVSYL EGSTASLRCF LQLRDATPGG AIVSELCQAL SSSHCRVLLI TPGFLQDPWC KYQMLQALTE APGAEGCTIP LLSGLSRAAY PPELRFMYYV DGRGPDGGFR QVKEAVMRYL QTLS

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:

CD93 Human Recombinant

CD93 Molecule, CD93 Antigen, Complement Component 1, Q Subcomponent, Receptor 1, Complement Component 1 Q Subcomponent Receptor 1, Matrix-Remodeling-Associated Protein 4, Matrix-Remodelling Associated 4, C1q/MBL/SPA Receptor, C1qR(P), C1Qrp, C1QR1, MXRA4, CDw93, C1qR, C1q Receptor 1, DJ737E23.1, ECSM3.

Product # :

PRO-2336

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Description

CD93 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 567 amino acids (22-580 aa) and having a molecular mass of 59.3kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions).CD93 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CD93 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CD93, is a receptor or else an element of a larger receptor complex for C1q, MBL2-mannose-binding lectin and SPA-pulmonary surfactant protein A. CD93 mediates the enhancement of phagocytosis in monocytes as well as macrophages upon interaction with soluble defense collagens. CD93 takes part in the intercellular adhesion. Furthermore, CD93 was expressed on (pre) plasmablasts/plasma cells, including long-lived plasma cells which demonstrated decreased cell cycle activity, high levels of isotype-switched Ig secretion, as well as modification of the transcriptional network. CD93 is vital for the maintenance of plasma cells in bone marrow niches.
Synonyms
CD93 Molecule, CD93 Antigen, Complement Component 1, Q Subcomponent, Receptor 1, Complement Component 1 Q Subcomponent Receptor 1, Matrix-Remodeling-Associated Protein 4, Matrix-Remodelling Associated 4, C1q/MBL/SPA Receptor, C1qR(P), C1Qrp, C1QR1, MXRA4, CDw93, C1qR, C1q Receptor 1, DJ737E23.1, ECSM3.
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
TGADTEAVVC VGTACYTAHS GKLSAAEAQN HCNQNGGNLA TVKSKEEAQH VQRVLAQLLR REAALTARMS KFWIGLQREK GKCLDPSLPL KGFSWVGGGE DTPYSNWHKE LRNSCISKRC VSLLLDLSQP LLPSRLPKWS EGPCGSPGSP GSNIEGFVCK FSFKGMCRPL ALGGPGQVTY TTPFQTTSSS LEAVPFASAA NVACGEGDKD ETQSHYFLCK EKAPDVFDWG SSGPLCVSPK YGCNFNNGGC HQDCFEGGDG SFLCGCRPGF RLLDDLVTCA SRNPCSSSPC RGGATCVLGP HGKNYTCRCP QGYQLDSSQL DCVDVDECQD SPCAQECVNT PGGFRCECWV GYEPGGPGEG ACQDVDECAL GRSPCAQGCT NTDGSFHCSC EEGYVLAGED GTQCQDVDEC VGPGGPLCDS LCFNTQGSFH CGCLPGWVLA PNGVSCTMGP VSLGPPSGPP DEEDKGEKEG STVPRAATAS PTRGPEGTPK ATPTTSRPSL SSDAPITSAP LKMLAPSGSP GVWREPSIHH ATAASGPQEP AGGDSSVATQ NNDGTDGQKV EHHHHHH

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:

Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

Product # :

PRO-1536

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Description

RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.
Synonyms
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

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, Sf9 Human Recombinant

Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.

Product # :

CYT-1058

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Description

IL12 Mouse Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-335aa, total of 319 aa, MW 35.7kDa) and IL12B (23-215aa, total of 199 aa, MW 22.5kDa), having a total predicted molecular mass of 58.3kDa (Molecular weight on SDS-PAGE will appear higher). IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL12 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

SDS-PAGE

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Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is a crucial part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
Synonyms
Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.
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.
Amino Acid Sequence
IL12B(p40)
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
IL12A(p35)
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
VTINRVMGYL SSAHHHHHH.
Background
What is the molecular weight/Mw of IL12 MOUSE, SF9 Protein?
IL12 MOUSE, SF9 Protein has a total Mw of 58.3kDa.

What is the source or expression system of IL12 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of IL12 MOUSE, SF9 Protein?
IL12 MOUSE, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 MOUSE, SF9 Protein?
The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

What is the amino acid sequence of IL12 MOUSE, SF9 Protein?
IL12B(p40)
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
IL12A(p35)
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
VTINRVMGYL SSAHHHHHH.
What applications can IL12 MOUSE, SF9 Protein be used in?
IL12 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL12 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 MOUSE, 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 IL12 MOUSE, 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:

TIE1 Fc Chimera Mouse Recombinant

Tyrosine kinase with immunoglobulin-like and EGF-like domains 1, JTK14, TIE, TIE1.

Product # :

PKA-247

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Description

Soluble TIE-1 Mouse Recombinant fused with the Fc part of human IgG1 produced in CHO cells is a glycosylated disulfide-linked homodimeric polypeptide chain containing amino acids 23-749 and having a total molecular mass of 260kDa. The Mouse TIE-1/Fc monomer has a calculated molecular mass of approximately 105kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 130kDa protein in SDS-PAGE under reducing conditions.The TIE1 Fc Chimera is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

TIE-1 Fc Chimera was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1124 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 727 residue extracellular domain and a 354 residue cytoplasmic domain. Whereas two ligands have been described for TIE-2 [angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2)], so far no ligand was found for TIE-1.
Synonyms
Tyrosine kinase with immunoglobulin-like and EGF-like domains 1, JTK14, TIE, TIE1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized sTIE-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIE-1 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 TIE-1 Fc Chimera in sterile water 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:

Advanced Glycosylation End Product-Specific Receptor Mouse Recombinant

Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.

Product # :

PRO-2781

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Description

sRAGE Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 317 amino acids (Gly23–Asp333) and having a molecular mass of 34.0kDa. sRAGE Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Synonyms
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
GQNITARIGE PLVLSCKGAP KKPPQQLEWK LNTGRTEAWK VLSPQGGPWD SVARILPNGS LLLPATGIVD EGTFRCRATN RRGKEVKSNY RVRVYQIPGK PEIVDPASEL TASVPNKVGT CVSEGSYPAG TLSWHLDGKL LIPDGKETLV KEETRRHPET GLFTLRSELT VIPTQGGTHP TFSCSFSLGL PRRRPLNTAP IQLRVREPGP PEGIQLLVEP EGGIVAPGGT VTLTCAISAQ PPPQVHWIKD GAPLPLAPSP VLLLPEVGHE DEGTYSCVAT HPSHGPQESP PVSIRVTETG DEGPAEGEGL DHHHHHH.
Background
The soluble receptor for advanced glycation end products, sRAGE, is a multifunctional protein known for its involvement in diverse physiological processes, including inflammation, aging, and chronic diseases. Research using mouse models has been instrumental in unraveling the complexities of sRAGE biology and its implications for health and disease. This study aims to provide a comprehensive exploration of sRAGE in mouse physiology, shedding light on its various functions and potential applications in understanding aging and disease mechanisms.
The primary objective of this research is to elucidate the impact of sRAGE in mouse models on aging processes. In vivo experiments utilizing genetically modified mice with altered sRAGE expression will be conducted to investigate how sRAGE influences the aging process, including effects on tissue homeostasis, oxidative stress, and longevity. Understanding these mechanisms is fundamental for deciphering the role of sRAGE in age-related diseases.
The second objective is to assess the clinical relevance of sRAGE in mouse models of chronic diseases. Mouse models of diseases such as diabetes, Alzheimer's disease, and cancer will be employed to explore how sRAGE modulation affects disease progression, inflammation, and tissue damage. These investigations may provide valuable insights into potential therapeutic strategies targeting sRAGE in various chronic diseases.
The third objective is to explore the broader implications of sRAGE in mouse physiology, including its effects on immunity, tissue repair, and metabolic regulation. Research will investigate its roles in immune cell function, wound healing, and glucose homeostasis. Understanding the multifaceted properties of sRAGE in mouse models may open new avenues for therapeutic interventions in various health and disease contexts.
By delving into the diverse functions of sRAGE in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for age-related diseases and chronic conditions influenced by sRAGE.

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:

Staphylococcal Protein A 434 a.a Recombinant

Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

Product # :

PRO-686

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Description

Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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
MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.

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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

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

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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.

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Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description