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Description:

Dipeptidyl-Peptidase 4 Human Recombinant, HEK

CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

Product # :

ENZ-1187

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Description

DPP4 Human Recombinant is a single, glycosylated polypeptide chain containing 977 amino acids (29-766a.a) and having a molecular mass of 112.1kDa (calculated). DPP4 is fused to a 239 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

DPP4 protein solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

Biological Activity

Specific activity is > 15,000 pmol/min/ug in which one unit defined as the amount of enzyme that hydrolyze 1pmole of H-Gly-Pro-AMC.HBr to H-Gly-Pro and AMC per minute at pH 8.0 at 37℃.

The ED50 range ≤250 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike S1 Subunit (CAT# sars-052)..

The ED50 range ≤200 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike RBD (CAT# sars-054).

The ED50 range ≤120 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike (CAT# sars-051).

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Synonyms
CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.
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
DGSMNKGTDD ATADSRKTYT LTDYLKNTYR LKLYSLRWIS DHEYLYKQEN NILVFNAEYG NSSVFLENST FDEFGHSIND YSISPDGQFI LLEYNYVKQW RHSYTASYDI YDLNKRQLIT EERIPNNTQW VTWSPVGHKL AYVWNNDIYV KIEPNLPSYR ITWTGKEDII YNGITDWVYE EEVFSAYSAL WWSPNGTFLA YAQFNDTEVP LIEYSFYSDE SLQYPKTVRV PYPKAGAVNP TVKFFVVNTD SLSSVTNATS IQITAPASML IGDHYLCDVT WATQERISLQ WLRRIQNYSV MDICDYDESS GRWNCLVARQ HIEMSTTGWV GRFRPSEPHF TLDGNSFYKI ISNEEGYRHI CYFQIDKKDC TFITKGTWEV IGIEALTSDY LYYISNEYKG MPGGRNLYKI QLSDYTKVTC LSCELNPERC QYYSVSFSKE AKYYQLRCSG PGLPLYTLHS SVNDKGLRVL EDNSALDKML QNVQMPSKKL DFIILNETKF WYQMILPPHF DKSKKYPLLL DVYAGPCSQK ADTVFRLNWA TYLASTENII VASFDGRGSG YQGDKIMHAI NRRLGTFEVE DQIEAARQFS KMGFVDNKRI AIWGWSYGGY VTSMVLGSGS GVFKCGIAVA PVSRWEYYDS VYTERYMGLP TPEDNLDHYR NSTVMSRAEN FKQVEYLLIH GTADDNVHFQ QSAQISKALV DVGVDFQAMW YTDEDHGIAS STAHQHIYTH MSHFIKQCFS LPKLLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGK.
Background
DPP4 protein, also known as Dipeptidyl peptidase-4 or CD26, is a cell surface protease with diverse functions in cell signaling and metabolism. This research aims to investigate the role of DPP4 protein in various physiological processes and its implications in disease pathogenesis. Understanding the biological significance of DPP4 can provide insights into its potential as a therapeutic target for several disorders.
Function of DPP4 Protein:
DPP4 protein is involved in the cleavage and regulation of several peptide hormones and chemokines, influencing their bioactivity and half-life. It is widely expressed in various tissues, including immune cells, endothelial cells, and epithelial cells. DPP4 can modulate immune responses, glucose metabolism, and neuropeptide signaling through enzymatic and non-enzymatic activities.
Role of DPP4 Protein in Immune Regulation:
DPP4 protein plays a role in immune cell activation and regulation. It is expressed on the surface of T cells, where it functions as a co-stimulatory molecule. DPP4 engagement on T cells promotes T cell activation, cytokine production, and adhesion to endothelial cells. Additionally, DPP4 can cleave and inactivate certain chemokines, thereby influencing chemotaxis and immune cell recruitment.
Implications of DPP4 Protein in Metabolic Disorders:
DPP4 protein is involved in glucose metabolism and insulin regulation. It cleaves incretin hormones, such as glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP), which play crucial roles in glucose homeostasis. Inhibition of DPP4 activity can enhance the action of these incretin hormones, leading to improved glycemic control. Therefore, DPP4 inhibitors have been developed as antidiabetic drugs.
Association of DPP4 Protein with Cardiovascular Diseases:
DPP4 protein has been implicated in the pathogenesis of cardiovascular diseases. Elevated DPP4 levels have been observed in patients with heart failure, atherosclerosis, and hypertension. DPP4 can contribute to endothelial dysfunction, inflammation, and vascular remodeling, which are key factors in the development and progression of cardiovascular disorders. Inhibition of DPP4 activity has shown potential as a therapeutic strategy in preclinical studies.
Given its involvement in various biological processes and disease pathogenesis, DPP4 protein has emerged as a potential therapeutic target. DPP4 inhibitors, which prevent the enzymatic activity of DPP4, have been developed for the treatment of type 2 diabetes. These inhibitors enhance the action of incretin hormones, leading to improved glycemic control. Additionally, ongoing research aims to explore the therapeutic potential of DPP4 inhibitors in other conditions, such as immune-mediated disorders and cardiovascular diseases.
Conclusion:
The investigation of DPP4 protein provides insights into its diverse functions in cell signaling, immune regulation, and metabolism. Understanding the role of DPP4 in disease pathogenesis opens avenues for the development of targeted therapies for conditions such as diabetes, cardiovascular diseases, and immune-mediated disorders. Further research on DPP4 protein and its associated pathways may uncover new therapeutic opportunities and improve patient outcomes.

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

Description:

Bone Marrow Stromal Cell Antigen 1 Human Recombinant

Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

Product # :

CYT-1071

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Description

BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.

What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.

What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.

What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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:

Granulocyte-Colony Stimulating Factor Rat Recombinant

Granulocyte colony stimulating factor, Protein Csf3, Csf3.

Product # :

CYT-940

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Description

GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

Purity

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

Biological Activity

The ED₅₀ determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 10⁷ IU/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 the GCSF 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
Granulocyte colony stimulating factor, Protein Csf3, Csf3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 GCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.
Background
What is the molecular weight/Mw of G CSF RAT Protein?
G CSF RAT Protein has a total Mw of 21.5kDa.

What is the source or expression system of G CSF RAT Protein?
Escherichia Coli.

What is the Purity of G CSF RAT Protein?
G CSF RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF RAT Protein?
The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

What is the amino acid sequence of G CSF RAT Protein?
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

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

What is the endotoxin level for G CSF RAT Protein?
The endotoxin level is minimal, G CSF RAT 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:

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 Human Recombinant

Carcinoembryonic Antigen Related Cell Adhesion Molecule 1, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 (Biliary Glycoprotein), CD66a Antigen, BGP1, BGP, Biliary Glycoprotein 1, Antigen CD66, BGP-1, BGPI.

Product # :

PRO-2352

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Description

CEACAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 405 amino acids (35-428 a.a.) and having a molecular mass of 44.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-70 kDa). CEACAM1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CEACAM1protein 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
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 (CEACAM1) belongs to the carcinoembryonic antigen (CEA) gene family which is a part of the immunoglobulin superfamily. CEACAM1 is a cell adhesion protein which mediates homophilic cell adhesion in a calcium-independent way. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. CEACAM1 functions as coinhibitory receptor in immune response, and plays a role also as an activator during angiogenesis.
Synonyms
Carcinoembryonic Antigen Related Cell Adhesion Molecule 1, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 (Biliary Glycoprotein), CD66a Antigen, BGP1, BGP, Biliary Glycoprotein 1, Antigen CD66, BGP-1, BGPI.
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
ADPEFQLTTE SMPFNVAEGK EVLLLVHNLP QQLFGYSWYK GERVDGNRQI VGYAIGTQQA TPGPANSGRE TIYPNASLLI QNVTQNDTGF YTLQVIKSDL VNEEATGQFH VYPELPKPSI SSNNSNPVED KDAVAFTCEP ETQDTTYLWW INNQSLPVSP RLQLSNGNRT LTLLSVTRND TGPYECEIQN PVSANRSDPV TLNVTYGPDT PTISPSDTYY RPGANLSLSC YAASNPPAQY SWLINGTFQQ STQELFIPNI TVNNSGSYTC HANNSVTGCN RTTVKTIIVT ELSPVVAKPQ IKASKTTVTG DKDSVNLTCS TNDTGISIRW FFKNQSLPSS ERMKLSQGNT TLSINPVKRE DAGTYWCEVF NPISKNQSDP IMLNVNYNAL PQENGLSPGH HHHHH.

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:

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 Human Recombinant

CEA, CGM2, Carcinoembryonic antigen CGM2.

Product # :

PRO-1483

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Description

CEACAM7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (36-242 a.a.) and having a molecular mass of 25.7kDa.CEACAM7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CEACAM7 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 (CEACAM7) is a member of the immunoglobulin superfamily, CEA family. CEACAM7 contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. CEACAM7 is intensely down-regulated in colonic adenocarcinomas.
Synonyms
CEA, CGM2, Carcinoembryonic antigen CGM2.
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 MGSTNIDVVP FNVAEGKEVL LVVHNESQNL YGYNWYKGER VHANYRIIGY VKNISQENAP GPAHNGRETI YPNGTLLIQN VTHNDAGIYT LHVIKENLVN EEVTRQFYVF SEPPKPSITS NNFNPVENKD IVVLTCQPET QNTTYLWWVN NQSLLVSPRL LLSTDNRTLV LLSATKNDIG PYECEIQNPV GASRSDPVTL NVRYESVQAS.

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:

Pentraxin-3 Human Recombinant, HEK

TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

Product # :

PRO-2041

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Description

Pentraxin-3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Glu18-Ser381) containing a total of 370 amino acids, having a calculated molecular mass of 41kDa and fused to a 6 aa His tag at C-Terminus.

Source

HEK 293.

Formulation

PTX3 was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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 0.5 mg/ml and let the lyophilized pellet dissolve completely. PTX3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ENSDDYDLMY VNLDNEIDNG LHPTEDPTPC DCGQEHSEWD KLFIMLENSQ MRERMLLQAT DDVLRGELQR LREELGRLAE SLARPCAPGA PAEARLTSAL DELLQATRDA GRRLARMEGA EAQRPEEAGR ALAAVLEELR QTRADLHAVQ GWAARSWLPA GCETAILFPM RSKKIFGSVH PVRPMRLESF SACIWVKATD VLNKTILFSY GTKRNPYEIQ LYLSYQSIVF VVGGEENKLV AEAMVSLGRW THLCGTWNSE EGLTSLWVNG ELAATTVEMA TGHIVPEGGI LQIGQEKNGC CVGGGFDETL AFSGRLTGFN IWDSVLSNEE IRETGGAESC HIRGNIVGWG VTEIQPHGGA QYVSHHHHHH.

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

Description:

Resistin Mutant Human Recombinant

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

Product # :

CYT-585

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Description

9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

Source

Escherichia Coli.

Formulation

Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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
Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

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:

Thrombopoietin Mouse Recombinant, HEK

Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

Product # :

CYT-1157

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Description

TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293.

Formulation

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

Purity

Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

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Introduction
Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.
Synonyms
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 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
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH 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:

Desert HedgeHog (C23II) Human Recombinant, His Tag

HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

Product # :

CYT-763

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Description

DHH (C23II) His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (23-198) and having a molecular mass of 22.4kDa.DHH (C23II) His is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DHH (C23II) His solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
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 MGSMIIGPGR GPVGRRRYAR KQLVPLLYKQ FVPGVPERTL GASGPAEGRV ARGSERFRDL VPNYNPDIIF KDEENSGADR LMTERCKERV NALAIAVMNM WPGVRLRVTE GWDEDGHHAQ DSLHYEGRAL DITTSDRDRN KYGLLARLAV EAGFDWVYYE SRNHVHVSVK ADNSLAVRAG G

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:

Desert Hedgehog (C23II) Human Recombinant

HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

Product # :

CYT-362

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Description

DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×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 Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED₅₀ for this effect is 15-45 μg/ml.

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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

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 Mouse Recombinant, His Tag

Interleukin-6, IL-6.

Product # :

CYT-845

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Description

Interleukin-6 Mouse Recombinant produced in E.Coli migrates at 25kDa. Recombinant IL-6 Mouse is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

IL6 Mouse protein solution contains 25mM K2CO3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
Interleukin-6, IL-6.
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.
Background
Research Paper on Interleukin-6 Mouse Recombinant, His Tag
Abstract:
Interleukin-6 (IL-6) Mouse Recombinant, tagged with His, is a cornerstone in unraveling the intricate web of immune modulation. This research paper delves into its molecular intricacies and its profound implications in immunological research. Through an exploration of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its pivotal role in shaping immune responses.
Introduction:
IL-6 Mouse Recombinant, bearing a His tag, has emerged as a pivotal tool in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.
Molecular Features and His Tag Precision:
Unveiling the molecular structure of IL-6 Mouse Recombinant, His Tag, we recognize its significance in facilitating purification and characterization. The His tag enhances our ability to study its functions with precision.
Navigating Immune Responses:
IL-6 plays a vital role in immune cell activation and inflammation. IL-6 Mouse Recombinant, His Tag, enables researchers to delve deeper into the cytokine's functions, shedding light on its impact on immune dynamics.
Synonyms and Network Connections:
Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of cytokine-mediated signaling networks. IL-6 Mouse Recombinant, His Tag, contributes to our understanding of these interconnected pathways.
Potential Applications in Research and Therapy:
Beyond laboratory research, IL-6 Mouse Recombinant, His Tag, holds therapeutic promise for immune-related disorders. Its utility in investigating disease mechanisms and evaluating therapeutic interventions marks it as a versatile tool.
Clinical Implications and Future Avenues:
The clinical relevance of IL-6 Mouse Recombinant, His Tag, is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its potential as a therapeutic intervention opens avenues for novel treatment strategies.
Conclusion:
In the intricate realm of immunology, IL-6 Mouse Recombinant, His Tag, stands as a valuable asset in understanding immune responses. Its molecular precision, pivotal functions, and potential therapeutic implications position it as an indispensable tool for advancing our knowledge of immune regulation.

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:

ChaC Cation Transport Regulator Homolog 2 Human Recombinant

ChaC Cation Transport Regulator Homolog 2 (E. Coli), ChaC Cation Transport Regulator-Like 2 (E. Coli), Gamma-GCT Acting On Glutathione Homolog 2.

Product # :

PRO-1835

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Description

CHAC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184) and having a molecular mass of 23.3 kDa. CHAC2 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The CHAC2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cation transport regulator-like protein 2 (CHAC2) is a member of the chaC family. Catalyzes the cleavage glutathione into 5-oxoproline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Synonyms
ChaC Cation Transport Regulator Homolog 2 (E. Coli), ChaC Cation Transport Regulator-Like 2 (E. Coli), Gamma-GCT Acting On Glutathione Homolog 2.
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 MGSMWVFGYG SLIWKVDFPY QDKLVGYITN YSRRFWQGST DHRGVPGKPG RVVTLVEDPA GCVWGVAYRL PVGKEEEVKA YLDFREKGGY RTTTVIFYPK DPTTKPFSVL LYIGTCDNPD YLGPAPLEDI AEQIFNAAGP SGRNTEYLFE LANSIRNLVP EEADEHLFAL EKLVKERLEG KQNLNCI

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 Human Recombinant, His Tag

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

Product # :

CYT-484

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Description

IL-6 Human Recombinant produced in E.Coli migrates to 25kDa and is fused to a 6 amino acid his tag at its C-terminus. IL-6 is purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Interleukin-6 His-Tag protein is supplied in Phosphate buffered saline and 25mM K2CO3

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

More Info

Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
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.
Background
Research Paper on Interleukin-6 Human Recombinant, His Tag
Abstract:
Interleukin-6 (IL-6) Human Recombinant, tagged with His, serves as a cornerstone in unraveling the intricacies of immune modulation. This research paper delves into its molecular attributes and implications within immunological studies. Through an exploration of its functions, synonyms like DIF, TNFA, and TNFSF2, and potential applications, we gain insights into its pivotal role in shaping immune responses.
Introduction:
IL-6 Human Recombinant, bearing a His tag, holds a pivotal position in immunology research. This paper aims to comprehensively elucidate its molecular characteristics and its contribution to our understanding of immune mechanisms.
Molecular Structure and Insights:
Analyzing the molecular architecture of IL-6 Human Recombinant, His Tag, we unearth its pivotal role in immune signaling. Its interactions and functions contribute to orchestrating immune responses.
Navigating Immune Dynamics:
The well-established role of IL-6 in immune cell activation and inflammation forms a foundation. IL-6 Human Recombinant, His Tag, enables a deeper exploration of these immune processes, enriching our comprehension of cytokine-mediated functions.
Synonyms and Network Connections:
Understanding synonyms linked with IL-6, such as DIF, TNFA, and TNFSF2, enhances our grasp of immune signaling networks. IL-6 Human Recombinant, His Tag, plays a vital role in unraveling the intricacies of these interconnected pathways.
Potential Applications in Research and Beyond:
IL-6 Human Recombinant, His Tag, extends beyond research realms, holding promise in elucidating immune-related diseases. Its significance stretches to potential therapeutic interventions and diagnostic applications.
Clinical Implications and Future Prospects:
The clinical relevance of IL-6 Human Recombinant, His Tag, is underscored by its role in diseases marked by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for innovative strategies in disease management.
Conclusion:
Within the landscape of immunology, IL-6 Human Recombinant, His Tag, stands as a vital tool. Its molecular insights, fundamental functions, and potential implications position it as a cornerstone in advancing our understanding of immune regulation.

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 1a Human Recombinant

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

Product # :

CYT-236

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Description

IFN-beta 1a Human Recombinant produced in CHO (Chinese Hamster Ovarian) cells is a single, glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 22500 Dalton.IFN-beta1a is purified by proprietary chromatographic techniques.

Source

CHO (Chinese Hamster Ovarian) cells.

Formulation

Lyophilized from a solution containing 91 mg Human Albumin, and 620 mg mannitol and 50mM Acetate acid pH 3.8.

Purity

Greater than 99.0% 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 270 x 10⁶ IU/mg.

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Introduction
IFN-beta has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.
Stability
Lyophilized IFN-beta 1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Beta1a 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 1a 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 IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein has a total Mw of 22.5kDa.

What is the source or expression system of IFN BETA 1A HUMAN Protein?
CHO (Chinese Hamster Ovarian) cells.

What is the Purity of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1A 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 270 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is composed from 166 amino acids.

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

What is the endotoxin level for IFN BETA 1A HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1A HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

IFN Beta Mouse Recombinant, His Tag

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

Product # :

CYT-651

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SDS-PAGE

Description

IFN beta Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (22-182 a.a.) and having a molecular mass of 22 kDa. Mouse IFN beta is fused to 21 amino acid at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IFN-Beta (0.25mg/ml) contains 20mM HEPES (pH6.0), 0.5M NaCl, 10% glycerol.

Purity

Greater than 95% as determined by Analysis by SDS-PAGE.

SDS-PAGE

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Introduction
IFN-beta 1b has antiviral, antibacterial and anticancer activities.
Influenza A viruses not only inhibit IFN-beta gene induction but also supress Type-I IFN signaling via mechanism involving induction of the SOCS-3 protein.
Intracellular bacteria and cytosolic poly (dA-dT) trigger IFN-beta responses in different human cells without requiring human ZBP1.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
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 MINYKQLQLQ ERTNIRKCQE LLEQLNGKIN LTYRADFKIP MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI VVRLLDELHQ QTVFLKTVLE EKQEERLTWE MSSTALHLKS YYWRVQRYLK LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF QN.
Background
What is the molecular weight/Mw of IFN B MOUSE, HIS Protein?
IFN B MOUSE, HIS Protein has a total Mw of 22kDa.

What is the source or expression system of IFN B MOUSE, HIS Protein?
Escherichia Coli.

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

What is the Biological Activity of IFN B MOUSE, HIS Protein?
The biological functionality of IFN B MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of IFN B MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MINYKQLQLQ ERTNIRKCQE LLEQLNGKIN LTYRADFKIP MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI VVRLLDELHQ QTVFLKTVLE EKQEERLTWE MSSTALHLKS YYWRVQRYLK LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF QN.

What applications can IFN B MOUSE, HIS Protein be used in?
IFN B MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN B MOUSE, HIS Protein?
The endotoxin level is minimal, IFN B MOUSE, 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:

Clusterin Rat Recombinant

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

Product # :

CYT-437

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Description

The Clusterin Rat His-Tagged Fusion Protein, produced in E.coli, is 26.5kDa protein containing 215 amino acid residues of the APO-J Rat and 25 additional amino acid residues: N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). (Underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.02M Tris buffer and 0.05M NaCl, pH 7.5.

Purity

Greater than 90% as determined by SDS PAGE.

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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.
Physical Appearance
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 a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.
Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 26.5kDa.

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

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

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

What is the amino acid sequence of CLUSTERIN Protein?
MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.

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

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

Resistin Human Recombinant, His Tag

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

Product # :

CYT-256

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Description

Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Physical Appearance
Sterile filtered 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.

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:

KISS-1 Metastasis-Suppressor Human Recombinant

Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.

Product # :

PRO-419

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Description

KISS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (20-138) and having a molecular mass of 12.6 Dalton. The KISS1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
KISS1 is a metastasis suppressor protein that suppresses metastases of melanomas and breast carcinomas without affecting tumorigenicity.KISS1 functions to inhibit chemotaxis and invasion, attenuating metastasis in malignant melanomas. KISS1 is involved in the regulation of cell-matrix adhesion. KISS1 plays a role in cytoskeletal reorganization. A polymorphism in the terminal exon of KISS1 mRNA results in two protein isoforms. Expression of KiSS1 is localized to specific regions of the hypothalamus in numerous species and is regulated by gonadal steroids and across the estrous cycle..KISS1 generates a c-terminally amidated peptide, metastin which functions as the endogenous ligand of the g-protein coupled receptor gpr54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.
Synonyms
Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.
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).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MEPLEKVASV GNSRPTGQQL ESLGLLAPGE QSLPCTERKP AATARLSRRG TSLSPPPESS GSPQQPGLSA PHSRQIPAPQ GAVLVQREKD LPNYNWNSFG LRFGKREAAP GNHGRSAGRG.

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:

Adiponectin Human Recombinant, Trimeric form

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-233

Price :

Quantity :

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biological activity
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Description

Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.

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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Adiponectin 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
Add deionized water to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

What is the Biological Activity of ADIPONECTIN Protein?
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.

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

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

Resistin Human Recombinant

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

Product # :

CYT-456

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Resistin Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 93 amino acids and having a total molecular weight of 19.7kDa.The Resistin Human Recombinant protein is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Sterile filtered and lyophilized from 0.1% Trifluoroacetic Acis (TFA).

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Physical Appearance
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 reconstitute the lyophilized Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP

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:

SIL1 Human Recombinant

SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.

Product # :

PRO-1187

Price :

Quantity :

Shipping Method :

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Description

SIL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 439 amino acids (32-461) and having a molecular mass of 50.0 kDa.SIL1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SIL1 is localized to endoplasmic reticulum (ER). SIL1 is an N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. SIL1 acts as a nucleotide exchange factor for another unfolded protein response protein. Mutations in SIL1 are linked to Marinesco-Sjogren syndrome.
Synonyms
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
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
MHQNLKEFAL TNPEKSSTKE TERKETKAEE ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL RLEHHHHHH.

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:

Coronavirus 2019 Nucleocapsid (1-419 a.a.), Biotinylated Recombinant

Product # :

SARS-036

Price :

Quantity :

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source
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Description

The HEK293 derived recombinant biotinylated protein contains the Coronavirus 2019 CoV-2 Nucleocapsid, Wuhan-Hu-1 strain, amino acids 1-419 fused to His-Avi tag at C-terminal.

Source

HEK293 Cells.

Formulation

CoV-2 Nucleocapsid protein is supplied in 50mM Tris, 0.15M NaCl & Arginine, pH7.5

Purity

Protein is >90% pure as determined SDS-PAGE.

More Info

Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cov-2 Nucleocapsid protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Nucleocapsid protein 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.
Purification Method
Purified by Metal-Afinity chromatographic technique.

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:

APRIL Human Recombinant

Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

Product # :

CYT-815

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sds-page

Description

APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.
Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
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
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
Background
APRIL Human Recombinant: Expanding the Horizons of Immunotherapy
Abstract:

APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.
Introduction:

Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.
APRIL Structure and Function:

APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.
Immunotherapeutic Applications of APRIL Human Recombinant:

APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.
Challenges and Future Directions:

Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.
Conclusion:

APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.
What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 17.6kDa.

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

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

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

What is the amino acid sequence of APRIL Protein?
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

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

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

Copper Chaperone for Superoxide Dismutase Human Recombinant

Superoxide dismutase copper chaperone, Copper chaperone for superoxide dismutase.

Product # :

PRO-251

Price :

Quantity :

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Shipped with Ice Packs

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Description

CCS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294amino acids (1-274a.a.) and having a molecular wieght of 31.2kDa. The CCS is fused to a 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCS protein solution (1mg/1ml) contains 20 mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.2M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CCS is vital for the integration of copper into SOD-1, and as a result is needed for its enzymatic activity. CCS inhibits copper ions from binding to intracellular copper scavengers and provides the SOD-1 enzyme with the required copper cofactor. CCS escorts copper just to SOD-1 and is unable to deliver copper to proteins in the mitochondria, nucleus or secretory pathway. Although many tissues express CCS, the chaperone is most abundant in the kidney, liver and Purkinje cells in the neuropil of the central nervous system.
Synonyms
Superoxide dismutase copper chaperone, Copper chaperone for superoxide dismutase.
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 MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL.

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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