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1000 results found for “prohibitin”
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Name :
BCDIN3D HumanDescription:
BCDIN3D Human Recombinant
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
Product # :
PRO-1262Price :
Quantity :
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Shipped with Ice Packs
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Description
BCDIN3D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292 a.a) and having a molecular mass of 35kDa.BCDIN3D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCDIN3D protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
BCDIN3D is a member of the methyltransferase superfamily and contains 1 Bin3-type SAM domain. BCDIN3D acts in the catalysis of the transfer of a methyl group to an acceptor molecule. BCDIN3D is an O-methyltransferase which specifically dimethylates the 5' monophosphate of pre-miRNAs, serving as a negative regulator of miRNA processing. BCDIN3D mediates the methylation of pre-miR-145, as well as other pre-miRNAs.
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Synonyms
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPTEL DGGSVKETAA EEESRVLAPG AAPFGNFPHY SRFHPPEQRL RLLPPELLRQ LFPESPENGP ILGLDVGCNS GDLSVALYKH FLSLPDGETC SDASREFRLL CCDIDPVLVK RAEKECPFPD ALTFITLDFM NQRTRKVLLS SFLSQFGRSV FDIGFCMSIT MWIHLNHGDH GLWEFLAHLS SLCHYLLVEP QPWKCYRAAA RRLRKLGLHD FDHFHSLAIR GDMPNQIVQI LTQDHGMELI CCFGNTSWDR SLLLFRAKQT IETHPIPESL IEKGKEKNRL SFQKQ.
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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Name :
BST1 HumanDescription:
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-1071Price :
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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.
More Info
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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.
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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.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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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.
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Name :
IL 7 Human, YeastDescription:
Interleukin-7 Human Recombinant, Yeast
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-298Price :
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Description
Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.More Info
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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-7 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.
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Name :
C19ORF80 HumanDescription:
Chromosome 19 Open Reading Frame 80 Human Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-1575Price :
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Shipped at Room temp
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Description
C19ORF80 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-198) containing 187 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.1kDa (calculated).
Source
Escherichia Coli.
Formulation
C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASAPMGGPELAQ HEELTLLFHG TLQLGQALNG VYRTTEGRLT KARNSLGLYG RTIELLGQEV SRGRDAAQEL RASLLETQME EDILQLQAEA TAEVLGEVAQ AQKVLRDSVQ RLEVQLRSAW LGPAYREFEV LKAHADKQSH ILWALTGHVQ RQRREMVAQQ HRLRQIQERL HTAALPA.
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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Name :
ULBP1 Human, Sf9Description:
UL16 Binding Protein 1 Human Recombinant, Sf9
UL16 Binding Protein 1, Retinoic Acid Early Transcript 1I, alcan-beta, NKG2D Ligand 1, NKG2DL1, RAET1I, N2DL-1, NKG2D ligand 1, ULBP.
Product # :
CYT-996Price :
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Description
ULBP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (26-216) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 20-40kDa).ULBP1 is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ULBP1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
ULBP1 together with at least ULBP2 and ULBP3, is ligand for the NKG2D receptor. ULBPs stimulate various signaling pathways in primary NK cells, which result in cytokines and chemokines production. In CMV infected cells, ULBP1 cooperates with soluble CMV glycoprotein UL16 to inhibit the interaction with the NKG2D receptor providing a mechanism by which CMV infected cells escape the immune system. Additionally, UL16 retains ULBP1 to the ER and cis-Golgi apparatus to prevent it from reaching cell surface.
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Synonyms
UL16 Binding Protein 1, Retinoic Acid Early Transcript 1I, alcan-beta, NKG2D Ligand 1, NKG2DL1, RAET1I, N2DL-1, NKG2D ligand 1, ULBP.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
ADLGWVDTHC LCYDFIITPK SRPEPQWCEV QGLVDERPFL HYDCVNHKAK AFASLGKKVN VTKTWEEQTE TLRDVVDFLK GQLLDIQVEN LIPIEPLTLQ ARMSCEHEAH GHGRGSWQFL FNGQKFLLFD SNNRKWTALH PGAKKMTEKW EKNRDVTMFF QKISLGDCKM WLEEFLMYWE QMLDPTKPPS LAPGHHHHHH.
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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Name :
MAPT Human 381a.a.Description:
Microtubule-Associated Protein Tau 381 a.a. Human Recombinant
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-042Price :
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Description
MAPT Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 41.8kDa. The NCBI Accession No. is EAW93573.1.The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.
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Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY
KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L.
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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Name :
RAB3A HumanDescription:
RAB3A, Member RAS Oncogene Family Human Recombinant
Ras-related protein Rab-3A, RAB3A.
Product # :
PRO-870Price :
Quantity :
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Shipped with Ice Packs
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Description
RAB3A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-220 a.a) and having a molecular mass of 27.1kDa.RAB3A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RAB3A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Rab3A is a member of the small GTPase superfamily, Rab family. Rab3A is a small, Ras-like GTPase expressed in neuroendocrine cells, in which Rab3A is linked with secretory vesicle membranes and regulates exocytosis. Rab3A protein may have a role in neurotransmitter release by regulating membrane flow in the nerve terminal.
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Synonyms
Ras-related protein Rab-3A, RAB3A.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV DVICEKMSES LDTADPAVTG AKQGPQLSDQ QVPPHQDCAC.
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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Name :
RAB6A HumanDescription:
RAB6A, Member RAS Oncogene Family Human Recombinant
Ras-related protein Rab-6A, Rab-6, RAB6A, RAB6, RAB6B, RAB6A'.
Product # :
PRO-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RAB6A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-208) and having a molecular mass of 26.1kDa. RAB6A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAB6A solution (1 mg/ml) contains 20mM Tris buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RAB6A is a member of the small GTPase superfamily. RAB6A may be involved in protein transport. RAB6A is a regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) and has a low GTPase activity.
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Synonyms
Ras-related protein Rab-6A, Rab-6, RAB6A, RAB6, RAB6B, RAB6A'.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTGGD FGNPLRKFKL VFLGEQSVGK TSLITRFMYD SFDNTYQATI GIDFLSKTMY LEDRTIRLQL WDTAGQERFR SLIPSYIRDS AAAVVVYDIT NVNSFQQTTK WIDDVRTERG SDVIIMLVGN KTDLADKRQV SIEEGERKAK ELNVMFIETS AKAGYNVKQL FRRVAAALPG MESTQDRSRE DMIDIKLEKP QEQPVSEGGC SC.
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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Name :
GHRP6Description:
Growth Hormone Releasing Peptide-6
GHRP-6, GHRP6
Product # :
HOR-298Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Releasing Peptide-6 Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 873 Dalton and a Molecular formula of C46H56N12O6.
Formulation
The GHRP-6 peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by analysis by RP-HPLC.
More Info
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Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH act directly on pituitary somatotrophs to stimulate GH release. Growth hormone (GH) release is stimulated by a variety of synthetic secretagogues, of which growth hormone-releasing hexapeptide (GHRP-6) has been most thoroughly studied; it is thought to have actions at both pituitary and hypothalamic site.
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Synonyms
GHRP-6, GHRP6
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Releasing Peptide-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP-6 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.
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Solubility
It is recommended to reconstitute the lyophilized GHRP-6 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
His-D-Trp-Ala-Trp-D-Phe-Lys-NH2.
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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Name :
Bet v 2.0101Description:
Profilin-1 Recombinant
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
Product # :
PRO-2283Price :
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Shipped with Ice Packs
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Description
Recombinant Profilin-1 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 15,625 Dalton. Bet v 2.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bet v 2.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.
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Synonyms
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
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Physical Appearance
Sterile Filtered clear solution.
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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. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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.
- View Data Sheet
Name :
HCV CocktailDescription:
Hepatitis C Virus Cocktail Recombinant
Product # :
HCV-015Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
Recombinant HCV cocktail contains the recombinant hepatitis C virus core, NS3, NS4, NS5 proteins.
Source
Escherichia Coli.
Formulation
HCV Cocktail solution contains 25mM K2CO3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
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.
-
Applications
ELISA and lateral flow immunoassay.
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Background
Hepatitis C virus (HCV) is a major global health concern, with approximately 71 million people infected worldwide. Chronic HCV infection can lead to liver cirrhosis, hepatocellular carcinoma, and other severe liver-related complications. The nonstructural proteins NS3, NS4, and NS5 of HCV play critical roles in viral replication, assembly, and immune evasion, making them attractive targets for antiviral interventions. This research aims to characterize the recombinant forms of HCV NS3, NS4, and NS5 proteins to gain insights into their functional properties and identify potential targets for the development of effective antiviral strategies.
The primary objective of this study is to express and purify recombinant HCV NS3, NS4, and NS5 proteins using suitable expression systems. Recombinant DNA techniques will be employed to generate expression vectors harboring the respective genes, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant proteins will be purified using affinity chromatography or other appropriate methods, enabling subsequent biochemical and biophysical characterization.
The second objective is to investigate the roles of NS3, NS4, and NS5 proteins in HCV replication and assembly. In vitro assays will be performed to assess the enzymatic activities of NS3 protease and NS5 RNA-dependent RNA polymerase (RdRp). The effects of potential inhibitors or small molecules on these enzymatic activities will be evaluated. Furthermore, the interactions between NS4 protein and cellular components involved in viral assembly will be explored using protein-protein interaction assays.
The third objective is to determine the three-dimensional structures of the recombinant NS3, NS4, and NS5 proteins using techniques such as X-ray crystallography or cryo-electron microscopy. Structural information will provide valuable insights into the functional domains and potential binding sites within these proteins. These findings will aid in the design of novel antiviral compounds targeting specific regions of NS3, NS4, and NS5, with the goal of disrupting viral replication and assembly.
By characterizing the recombinant forms of HCV NS3, NS4, and NS5 proteins, this research aims to enhance our understanding of the molecular mechanisms underlying HCV infection. The insights gained from this study may contribute to the development of novel antiviral strategies targeting HCV, ultimately leading to improved therapeutic options for individuals affected by this persistent and debilitating viral infection.
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.
- View Data Sheet
Name :
CSTA Human, ActiveDescription:
Cystatin-A Human Recombinant, Active
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
Product # :
PRO-086Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cystatin A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 118 amino acids (1-98a.a.) and having a molecular mass of 13.1 kDa.The Cystatin A is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by reducing SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of CSTA on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.More Info
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Introduction
Human Cystatin A (CSTA or Stefin A) belongs to family 1 of the cystatin superfamily, which is characterized by the lack of disulphide bonds and carbohydrates. CSTA is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as Cathepsins B, H and L. Cystatin A has also been implicated in several disease states. Because of altered proteolytic state in cancer progression, CSTA may have a role in the proteolitic pathways.
-
Synonyms
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
-
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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.
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.
- View Data Sheet
Name :
MYCBP HumanDescription:
C-Myc Binding Protein Human Recombinant
C-Myc-binding protein, Associate of Myc 1, AMY-1, MYCBP, AMY1, FLJ41056.
Product # :
PRO-942Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MYCBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-103 a.a.) and having a molecular mass of 14.1kDa.MYCBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYCBP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
MYCBP is a member of the AMY1 family. MYCBP (c-Myc binding protein) binds to the transactivation domain of c-Myc and stimulates the activation of E-box-dependent transcription. MYCBP translocates from the cytoplasm to the nucleus during S phase when increased expression of c-Myc occurs. MYCBP also associates with AKAP 149 and AKAP 84 in mitochondria of somatic cells and sperm, suggesting a role for MYCBP in spermatogenesis. MYCBP is highly expressed in the heart, placenta, pancreas, skeletal muscle and kidney. It is also present at low levels in the lung.
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Synonyms
C-Myc-binding protein, Associate of Myc 1, AMY-1, MYCBP, AMY1, FLJ41056.
-
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 MAHYKAADSK REQFRRYLEK SGVLDTLTKV LVALYEEPEK PNSALDFLKH HLGAATPENP EIELLRLELA EMKEKYEAIV EENKKLKAKL AQYEPPQEEK RAE.
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.
- View Data Sheet
Name :
SNUPN HumanDescription:
Snurportin 1 Human Recombinant
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
Product # :
PRO-866Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SNUPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.3 kDa. The SNUPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNUPN Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β. -
Synonyms
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
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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 MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS
TPKLKGSSHS PDHPGCLMEN.
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.
- View Data Sheet
Name :
SSBP1Description:
Single-Stranded DNA Binding Protein 1 Sulfolobus solfataricus Recombinant
Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.
Product # :
PRO-359Price :
Quantity :
Shipping Method :
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Description
Recombinant Sulfolobus solfataricus Single-Stranded DNA Binding Protein 1 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 148 amino acids and having a molecular mass of 16.1kDa. The SSBP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SSBP1 is a 0.2µm filtered concentrated solution which contains 20mM Tris, pH 7.4, 200mM NaCl, 1mM EDTA, 0.5mM DTT, and 50% Glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.
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Synonyms
Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.
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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.
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Amino Acid Sequence
MEEKVGNLKP NMESVNVTVR VLEASEARQI QTKNGVRTIS EAIVGDETGR VKLTLWGKHA GSIKEGQVVK IENAWTTAFK GQVQLNAGSK TKIAEASEDG FPESSQIPEN TPTAPQQMRG GGRGFRGGGR RYGRRGGRRQ ENEEGEEE
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.
- View Data Sheet
Name :
Placental Lactogen OvineDescription:
Placental Lactogen Ovine Recombinant
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
Product # :
CYT-512Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Placental Lactogen Ovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Placental Lactogen Ovine is biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors. -
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Placental Lactogen Ovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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.
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Solubility
It is recommended to reconstitute the lyophilized Placental Lactogen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.85 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).
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.
- View Data Sheet
Name :
UBE2L6 HumanDescription:
Ubiquitin Conjugating Enzyme E2L 6 Human Recombinant
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
Product # :
ENZ-347Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBE2L6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a.) & having a molecular mass of 21.7 kDa. The UBE2L6 is fused to a 36 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris pH-8, 0.1mM PMSF, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.
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Synonyms
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASM RVVKELEDLQ KKPPPYLRNL SSDDANVLVW HALLLPDQPP YHLKAFNLRI SFPPEYPFKP PMIKFTTKIY HPNVDENGQI CLPIISSENW KPCTKTCQVL EALNVLVNRP NIREPLRMDL ADLLTQNPEL FRKNAEEFTL RFGVDRPS.
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.
- View Data Sheet
Name :
MBL2 HumanDescription:
Mannose-Binding Lectin 2 Human Recombinant
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
Product # :
PRO-1285Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.
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Synonyms
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.
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.
- View Data Sheet
Name :
CRHBP (22-322), HumanDescription:
Corticotropin Releasing Hormone Binding Protein (22-322 a.a.) Human Recombinant
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
Product # :
HOR-025Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRHBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (22-322 a.a) and having a molecular mass of 36.1kDa.CRHBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRHBP protein (1mg/ml) contains 10% glycerol, 0.4M urea and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.
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Synonyms
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSESRYLEL REAADYDPFL LFSANLKREL AGEQPYRRAL RCLDMLSLQG QFTFTADRPQ LHCAAFFISE PEEFITIHYD QVSIDCQGGD FLKVFDGWIL KGEKFPSSQD HPLPSAERYI DFCESGLSRR SIRSSQNVAM IFFRVHEPGN GFTLTIKTDP NLFPCNVISQ TPNGKFTLVV PHQHRNCSFS IIYPVVIKIS DLTLGHVNGL QLKKSSAGCE GIGDFVELLG GTGLDPSKMT PLADLCYPFH GPAQMKVGCD NTVVRMVSSG KHVNRVTFEY RQLEPYELEN PNGNSIGEFC LSGL
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.
- View Data Sheet
Name :
PROK Tritirachium albumDescription:
Tritirachium album Proteinase-K Recombinant
Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.
Product # :
ENZ-1015Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
Recombinant Tritirachium album Proteinase-K expressed in yeast containing 285 amino acids having a Mw of 29.3 kDa is purified by standard chromatography techniques.
Source
Yeast
Formulation
The Proteinase-K was lyophilized without any additives.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
36 Units/mg.
One unit is defined as the amount of enzyme that will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 mol tyrosine per min at 37°C, pH 7.5 (color by Folin-Ciocalteu reagent).More Info
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Introduction
The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.
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Synonyms
Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.
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Physical Appearance
Sterile Filtered lyophilized powder.
-
Stability
Recombinant Proteinase-K although stable at room temperature, should be stored between 2-8°C. Do not freeze!
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Solubility
It is recommended to reconstitute the lyophilized Proteinase-K in 20mM Tris-HCl (pH 7.4~8.0), 1mM CaCl2, 50% glycerol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Note
Bulk Proteinase-K recombinant is available 1,000 grams price is $100 per gram
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.
- View Data Sheet
Name :
IDH1Description:
Isocitrate Dehydrogenase-1 Yeast Recombinant
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Product # :
ENZ-289Price :
Quantity :
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Description
Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression. The ICDH is purified by proprietary chromatographic techniques.
Source
Yeast cells.
Formulation
One ml of solution contains 0.075 mol/l KPO4, 50% Glycerol, pH 7.1.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 115 U/mg.More Info
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Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
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Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
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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.
-
Unit Definition
One unit is defined as 1 µmol of NAD+ production per minute under the assay conditions (25°C, pH 7.5).
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.
- View Data Sheet
Name :
GH CarpDescription:
Growth Hormone Carp Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-297Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton. Growth Hormone Carp is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GH Carp was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth (Fine et al.1993). Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.More Info
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Introduction
Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Hormone Carp 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.
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Solubility
It is recommended to reconstitute the lyophilized Growth Hormone Carp recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and found to be Ser-Asp-Asn-Gln-Arg.
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.
- View Data Sheet
Name :
Kisspeptin-10Description:
Kisspeptin-10
Product # :
HOR-044Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
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Description
Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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.
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Solubility
It is recommended to reconstitute the lyophilized Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.
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Background
Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.
The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.
The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.
The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.
By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.
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.
- View Data Sheet
Name :
CST3 Protein, HisDescription:
Cystatin-C Human Recombinant, His Tag
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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.
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Solubility
Add deionized water to prepare a working stock solution of approximately 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.
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.