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1000 results found for “prefoldin”
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Name :
UPK2 HumanDescription:
Uroplakin 2 Human Recombinant
Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.
Product # :
PRO-479Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UPK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (26-155 a.a) and having a molecular mass of 16.2kDa.UPK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UPK2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Uroplakin 2 (UPK2) is one of the proteins of the highly urothelium-specific integral membrane proteins of the asymmetric unit membrane which forms urothelium apical plaques in mammals. The asymmetric unit membrane is thought to strengthen the urothelium by preventing cell rupture during bladder distention. The UPK2 protein is expressed in the peripheral blood of bladder cancer patients with transitional cell carcinomas.
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Synonyms
Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.
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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 MGSDFNISSL SGLLSPALTE SLLVALPPCH LTGGNATLMV RRANDSKVVT SSFVVPPCRG RRELVSVVDS GAGFTVTRLS AYQVTNLVPG TKFYISYLVK KGTATESSRE IPMSTLPRRN MESIGLGMAR TGG.
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 :
GTSF1 HumanDescription:
Gametocyte Specific Factor 1 Human Recombinant
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Product # :
PRO-561Price :
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Shipped with Ice Packs
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Description
GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
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Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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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
MGSSHHHHHH SSGLVPRGSH MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.
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 :
XPNPEP1 HumanDescription:
X-Prolyl Aminopeptidase-1 Human Recombinant
X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.
Product # :
ENZ-880Price :
Quantity :
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Shipped with Ice Packs
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Description
XPNPEP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 655 amino acids (1-623 a.a) and having a molecular mass of 73.4kDa. XPNPEP1 is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
XPNPEP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
X-Prolyl Aminopeptidase-1, also known as XPNPEP1 is a member of the peptidase M24B family. XPNPEP1 encodes the cytosolic form of a metalloaminopeptidase which catalyzes the cleavage of the N-terminal amino acid adjacent to a proline residue. Furthermore, XPNPEP1 plays a role in degradation as well as maturation of tachykinins, neuropeptides and peptide hormones.
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Synonyms
X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.
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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 MGSEFELRRQ ASMPPKVTSE LLRQLRQAMR NSEYVTEPIQ AYIIPSGDAH QSEYIAPCDC RRAFVSGFDG SAGTAIITEE HAAMWTDGRY FLQAAKQMDS NWTLMKMGLK DTPTQEDWLV SVLPEGSRVG VDPLIIPTDY WKKMAKVLRS AGHHLIPVKE NLVDKIWTDR PERPCKPLLT LGLDYTGISW KDKVADLRLK MAERNVMWFV VTALDEIAWL FNLRGSDVEH NPVFFSYAII GLETIMLFID GDRIDAPSVK EHLLLDLGLE AEYRIQVHPY KSILSELKAL CADLSPREKV WVSDKASYAV SETIPKDHRC CMPYTPICIA KAVKNSAESE GMRRAHIKDA VALCELFNWL EKEVPKGGVT EISAADKAEE FRRQQADFVD LSFPTISSTG PNGAIIHYAP VPETNRTLSL DEVYLIDSGA QYKDGTTDVT RTMHFGTPTA YEKECFTYVL KGHIAVSAAV FPTGTKGHLL DSFARSALWD SGLDYLHGTG HGVGSFLNVH EGPCGISYKT FSDEPLEAGM IVTDEPGYYE DGAFGIRIEN VVLVVPVKTK YNFNNRGSLT FEPLTLVPIQ TKMIDVDSLT DKECDWLNNY HLTCRDVIGK ELQKQGRQEA LEWLIRETQP ISKQH.
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 :
PRKAB1 HumanDescription:
Protein Kinase, AMP-Activated, Beta 1 non-Catalytic Subunit Human Recombinant
AMPK, HAMPKb, 5'-AMP-activated protein kinase subunit beta-1, AMPK subunit beta-1, AMPKb,PRKAB1.
Product # :
PKA-026Price :
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Shipped with Ice Packs
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Description
PRKAB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (1-270 a.a.) and having a molecular mass of 32.8 kDa. The PRKAB1 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PRKAB1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
5'-AMP-activated protein kinase subunit beta-1 (PRKAB1) hinders protein, carbohydrate and lipid biosynthesis, in addition to cell growth and proliferation. AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK acts via direct phosphorylation of metabolic enzymes, and longer-term effects by phosphorylation of transcription regulators. PRKAB1 is a regulator of cellular polarity by remodeling the actin cytoskeleton; most likely by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex compiles, through its C-terminus that joins alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
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Synonyms
AMPK, HAMPKb, 5'-AMP-activated protein kinase subunit beta-1, AMPK subunit beta-1, AMPKb,PRKAB1.
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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 MGSMGNTSSE RAALERHGGH KTPRRDSSGG TKDGDRPKIL MDSPEDADLF HSEEIKAPEK EEFLAWQHDL EVNDKAPAQA RPTVFRWTGG GKEVYLSGSF NNWSKLPLTR SHNNFVAILD LPEGEHQYKF FVDGQWTHDP SEPIVTSQLG TVNNIIQVKK TDFEVFDALM VDSQKCSDVS ELSSSPPGPY HQEPYVCKPE ERFRAPPILP PHLLQVILNK DTGISCDPAL LPEPNHVMLN HLYALSIKDG VMVLSATHRY KKKYVTTLLY KPI
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 :
ProInsulin HumanDescription:
ProInsulin C-Peptide Analogue Human Recombinant
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1120Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized ProInsulin C-Peptide Analogue 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
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.
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 :
LTA4H HumanDescription:
Leukotriene A4 Hydrolase Human Recombinant
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.
Product # :
ENZ-869Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.
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Synonyms
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.
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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 MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.
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 :
G CSF Human, PEGDescription:
Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-018Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.
Purity
Greater than 95.0% as determined by SEC-HPLC.
Biological Activity
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Colorless, clear and transparent solution.
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Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
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Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.
What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.
What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.
What applications can G CSF HUMAN, PEG Protein be used in?
G CSF HUMAN, PEG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Ketohexokinase HumanDescription:
Ketohexokinase Human Recombinant
KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.
Product # :
PKA-359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ketohexokinase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids and having a molecular mass of 32.7 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 1xPBS, pH 7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ketohexokinase catalyzes the phosphorylation of fructose to produce fructose-1-phosphate, resulting in the utilization of ATP and creation of AMP. Ketohexokinase commences initial step in the metabolism of dietary fructose and is a significant regulator of hepatic glucose metabolism. Ketohexokinase is found in liver, renal cortex, and small intestine. Its deficiency causes the benign hereditary metabolic disorder essential fructosuria, leading to fructose being excreted in the urine. Ketohexokinase-dependent metabolism of fructose induces proinflammatory mediators in proximal tubular cells. ketohexokinase plays an unknown physiologic function that remains intact in essential fructosuria. Ketohexokinase expression is reduceed in human clear cell type of renal cell carcinoma.
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Synonyms
KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.
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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
MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTIL SLLGAPCAFM GSMAPGHVAD FVLDDLRRYS VDLRYTVFQT TGSVPIATVI INEASGSRTI LYYDRSLPDV SATDFEKVDL TQFKWIHIEG RNASEQVKML QRIDAHNTRQ PPEQKIRVSV EVEKPREELF QLFGYGDVVF VSKDVAKHLG FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL HSDAFPPPRV VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV.
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 :
Cys-Protein-GDescription:
Cys-Protein G Recombinant
Product # :
PRO-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.
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Specificity
The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein 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.
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Name :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 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.
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Name :
HBsAg preS1Description:
Hepatitis B Surface Antigen, preS1 Recombinant
Product # :
HBS-871Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The E.Coli derived Recombinant Hepatitis B Surface Antigen preS1 is a single non-glycosylated polypeptide chain containing 119 amino acids and having a molecular weight of 12.6 kDa.
Source
Escherichia Coli.
Formulation
HBsAg protein was lyophilized from 0.2μm filtered (1mg/ml) solution in 20mM PB, pH 7.4, and 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
More Info
-
Introduction
Hepatitis B virus (HBV) is a human pathogen, causing serious liver disease. The HBV surface protein antigens (HBsAg) are comprised of three carboxyl co terminal HBs proteins termed large (LHBs), middle (MHBs) and small (SHBs, also called major) protein. LHBs and MHBs also share the highly hydrophobic, repetitive, membrane spanning S domain. In addition, LHBs has a 119 amino acid region called preS1.
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Stability
This lyophilized HBsAg preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
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Solubility
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGAN
SNNPDWDFNPNKDHWPEAHQVGAGAFGPGFTPPHGGLLGWSP
QAQGILTTVPVAPPPASTNRQSGRQPTPISPPLRDSHPQA. -
Purification Method
HBsAg protein was purified by proprietary 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.
- View Data Sheet
Name :
Protein-A/G CysDescription:
Protein A/G Cys Recombinant
Product # :
PRO-1928Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page, HPLC
Description
Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-A/G was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
-
Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.
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 :
TROVE2 Human, His BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, His Tag Biotinylated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2560Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
TROVE2 Human Recombinant Biotin produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 56kDa. The TROVE2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM HEPES (pH 8.0), 20% Glycerol and 150mM NaCl.
Purity
Greater than 89% as determined by Capillary Electrophoresis.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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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.
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 :
UMOD HumanDescription:
Uromodulin Human
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-381Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Uromodulin Human Native protein produced from Human Urine, is a glycosylated polypeptide chain having a total Mw of 80 kDa on SDS-PAGE.
Source
Human Urine.
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing deionized water.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at 2-8°C. DO NOT FREEZE!
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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.
- View Data Sheet
Name :
POLL HumanDescription:
Polymerase (DNA directed), Lambda Human Recombinant
Polymerase (DNA directed) lambda, Pol beta2, DNA polymerase beta-2, DNA polymerase kappa, BETAN, POLKAPPA, DNA polymerase beta-N, EC 2.7.7.7, EC 4.2.99.
Product # :
ENZ-182Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
POLL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300) and having a molecular mass of 36.0 kDa.POLL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The POLL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DNA polymerase POLL is involved in base excision repair (BER). POLL is a low-fidelity polymerase that takes part in both spontaneous and DNA damage-induced mutagenesis. Furthermore, POLL takes part in the mutagenic bypass of T-T dimers. Pol lambda possesses terminal transferase and 5’-deoxyribose-5-phosphate lyase activity which is synchronized by PCNA and replication protein A.
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Synonyms
Polymerase (DNA directed) lambda, Pol beta2, DNA polymerase beta-2, DNA polymerase kappa, BETAN, POLKAPPA, DNA polymerase beta-N, EC 2.7.7.7, EC 4.2.99.
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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 MLMHHQKYLQ RFLGGKREKK QKEACSIPGI GKRMAEKIIE ILESGHLRKL DHISESVPVL ELFSNIWGAG TKTAQMWYQQ GFRSLEDIRS QASLTTQQAI GLKHYSDFLE RMPREEATEI EQTVQKAAQA FNSGLLCVAC GSYRRGKATC GDVDVLITHP DGRSHRGIFS RLLDSLRQEG FLTDDLVSQE ENGQQQKYLG VCRLPGPGRR HRRLDIIVVP YSEFACALLY FTGSAHFNRS MRALAKTKGM SLSEHALSTA VVRNTHGCKV GPGRVLPTPT EKDVFRLLGL PYREPAERDW.
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 :
GLU-C S.aureusDescription:
Glutamyl endopeptidase Staphylococcal Recombinant
Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.
Product # :
ENZ-955Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- More Info
Description
Recombinant Staphylococcal GLU-C produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 267 amino acids and having a molecular mass of 28.9kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.
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Synonyms
Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized GLU-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLU-C 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 GLU-C in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA.
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 :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- biological activity
- More Info
Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.a.) 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 Oncostatin-M (209 a.a.) 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
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
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 :
CPA4 HumanDescription:
Carboxypeptidase A4 Human Recombinant
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
Product # :
ENZ-942Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
Description
CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CPA4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.
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Synonyms
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
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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
GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH HHH.
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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- biological activity
- More Info
- Activity
Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 Brain-derived Neurotrophic Factor 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.
- View Data Sheet
Name :
melA E. coliDescription:
Alpha-Galactosidase E.coli Recombinant
Mel-7, Alpha-galactosidase, b4119, JW4080.
Product # :
ENZ-609Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
melA E. coli Recombinant produced in E. coli is a single polypeptide chain containing 474 amino acids (1-451) and having a molecular mass of 53.0kDa.melA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The melA solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
melA is a member of the glycosyl hydrolase 4 family. melA catalyze the hydrolysis of saccharides containing o-1,6,-galactoside bonds. melA catalyze the same reaction in E.coli, human and yeast but is found in different cellular sections: The E.coli melA is a cytoplasmic protein and the human and yeast melA are secretory proteins. Thus, even though the active enzyme from all three species has almost an equal molecular weight, structural resemblances, as well as dissimilarities, are probable.
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Synonyms
Mel-7, Alpha-galactosidase, b4119, JW4080.
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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 MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR.
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 :
CSNK2A2 HumanDescription:
Casein Kinase 2, Alpha 2 Prime Human Recombinant
Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.
Product # :
PKA-042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSNK2A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 374 amino acids (1-350 a.a) and having a molecular mass of 43.7kDa. CSNK2A2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CSNK2A2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Casein kinase 2 subunit alpha (CSNK2A2) controls numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. CSNK2A2 protein functions as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response.
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Synonyms
Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.
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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 MGSHMPGPAA GSRARVYAEV NSLRSREYWD YEAHVPSWGN QDDYQLVRKL GRGKYSEVFE AINITNNERV VVKILKPVKK KKIKREVKIL ENLRGGTNII KLIDTVKDPV SKTPALVFEY INNTDFKQLY QILTDFDIRF YMYELLKALD YCHSKGIMHR DVKPHNVMID HQQKKLRLID WGLAEFYHPA QEYNVRVASR YFKGPELLVD YQMYDYSLDM WSLGCMLASM IFRREPFFHG QDNYDQLVRI AKVLGTEELY GYLKKYHIDL DPHFNDILGQ HSRKRWENFI HSENRHLVSP EALDLLDKLL RYDHQQRLTA KEAMEHPYFY PVVKEQSQPC ADNAVLSSGL TAAR.
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 :
CST4 Human, sf9Description:
Cystatin 4 Human Recombinant, sf9
Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.
Product # :
PRO-2250Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 131 amino acids (21-141 a.a.) and having a molecular mass of 15.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CST4 is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.
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Synonyms
Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.
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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
ADPMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEAHHHHH 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.
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Name :
DCTN2 (1-401) HumanDescription:
Dynactin 2 (1-401 a.a.) Human Recombinant
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
Product # :
PRO-1776Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (1-401 a.a) and having a molecular mass of 46.6kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
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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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEE LTSTSVEHII VNPNAAYDKF KDKRVGTKGL DFSDRIGKTK RTGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKTTVKES ATEEKLTPVL LAKQLAALKQ QLVASHLEKL LGPDAAINLT DPDGALAKRL LLQLEATKNS KGGSGGKTTG TPPDSSLVTY ELHSRPEQDK FSQAAKVAEL EKRLTELETA VRCDQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWSPIASTLP ELVQRLVTIK QLHEQAMQFG QLLTHLDTTQ QMIANSLKDN TTLLTQVQTT MRENLATVEG NFASIDERMK KLGK.
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 :
PPIL4 HumanDescription:
Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
Product # :
ENZ-026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PPIL4 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 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPIL solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.
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Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
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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 MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.
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.