Search results
1000 results found for “neurotrophic factors”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
OMP HumanDescription:
Olfactory Marker Protein Human Recombinant
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
Product # :
PRO-1412Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
OMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-163 a.a) and having a molecular mass of 21.3kDa. OMP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
OMP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Olfactory marker protein (OMP) which is expressed in the cytoplasm of olfactory chemosensory neurons in the nasal neuroepithelium, is associated in a unique way with the mature olfactory receptor neurons in numerous vertebrate species. OMP have a modulatory part in the odor detection/signal transduction cascade ant its expression is a sign of mature vertebrate olfactory receptor neurons (ORNs). OMP is also a potent enhancer of mitosis in fetal olfactory epithelial cells and it promotes an increase in uptake of tritiated thymidine in liver.
-
Synonyms
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
-
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 MGSMAEDRPQ QPQLDMPLVL DQGLTRQMRL RVESLKQRGE KRQDGEKLLQ PAESVYRLNF TQQQRLQFER WNVVLDKPGK VTITGTSQNW TPDLTNLMTR QLLDPTAIFW RKEDSDAIDW NEADALEFGE RLSDLAKIRK VMYFLVTFGE GVEPANLKAS VVFNQL.
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 :
CRCP HumanDescription:
CGRP Receptor Component Human Recombinant
CGRP receptor component protein, CGRP-RCP, RCP, RCP9, Calcitonin gene-related peptide-receptor component protein, RNA polymerase III subunit C9, DNA-directed RNA polymerase III subunit RPC9, HsC17, MGC111194.
Product # :
PRO-919Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CRCP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (1-148) and having a molecular mass of 19.0 kDa.The CRCP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRCP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
CRCP is a ubiquitous coupling protein for the calcitonin gene-related peptide and adrenomedullin receptors. CRCP controls ligand sensitivity in several tissues and has DNA-directed RNA polymerase activity, catalytic activity and calcitonin receptor activity.
-
Synonyms
CGRP receptor component protein, CGRP-RCP, RCP, RCP9, Calcitonin gene-related peptide-receptor component protein, RNA polymerase III subunit C9, DNA-directed RNA polymerase III subunit RPC9, HsC17, MGC111194.
-
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 MEVKDANSAL LSNYEVFQLL TDLKEQRKES GKNKHSSGQQ NLNTITYETL KYISKTPCRH QSPEIVREFL TALKSHKLTK AEKLQLLNHR PVTAVEIQLM VEESEERLTE EQIEALLHTV TSILPAEPEA EQKKNTNSNV AMDEEDPA
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 :
BCDIN3D HumanDescription:
BCDIN3D Human Recombinant
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
Product # :
PRO-1262Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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
-
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.
-
Synonyms
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
-
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 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.
- View Data Sheet
Name :
BSND HumanDescription:
Bartter Syndrome Infantile with Sensorineural Deafness Human Recombinant
Bartter Syndrome Infantile With Sensorineural Deafness (Barttin) , Deafness Autosomal Recessive 73, DFNB73, BART, barttin.
Product # :
PRO-1551Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BSND Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 290 amino acids (54-320) and having a molecular mass of 31.7kDa.BSND is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BSND solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
BSND is a vital beta subunit for CLC chloride channels. These heteromeric channels are restricted to basolateral membranes of renal tubules and of potassium-secreting epithelia of the inner ear. BSND gene mutations are linked with Bartter syndrome with sensorineural deafness.
-
Synonyms
Bartter Syndrome Infantile With Sensorineural Deafness (Barttin) , Deafness Autosomal Recessive 73, DFNB73, BART, barttin.
-
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 MGSCQCYPKI TFVPADSDFQ GILSPKAMGL LENGLAAEMK SPSPQPPYVR LWEEAAYDQS LPDFSHIQMK VMSYSEDHRS LLAPEMGQPK LGTSDGGEGG PGDVQAWMEA AVVIHKGSDE SEGERRLTQS WPGPLACPQG PAPLASFQDD LDMDSSEGSS PNASPHDREE ACSPQQEPQG CRCPLDRFQD FALIDAPTLE DEPQEGQQWE IALPNNWQRY PRTKVEEKEA SDTGGEEPEK EEEDLYYGLP DGAGDLLPDK ELGFEPDTQG
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 :
Epoetin Fc HumanDescription:
Erythropoietin-Alpha Fc-Chimera Human Recombinant
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Product # :
CYT-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized powder contains 1x PBS pH-7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.More Info
-
Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
-
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 140kDa.
What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
F7 HumanDescription:
Coagulation Factor VIIa Human Recombinant
Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.
Product # :
PRO-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Factor VIIa Human Recombinant produced in BHK is a glycosylated polypeptide two-chain dimer consisting of 406 amino acids with a molecular weight of 50kD.The Factor-VIIa is purified by proprietary chromatographic techniques.
Source
BHK cells (Baby Hamster Kidney Cells).
Formulation
The protein 1 mg/ml was lyophilized after from a sterile solution containing 10mg sucrose pH-6.
Purity
Greater than 98.0% as determined by analysis by SDS-PAGE.
Biological Activity
The potency per mg was tested and found to be 50,000Units/mg.More Info
-
Introduction
Coagulation factor VII is a vitamin K-dependent factor which is essential for hemostasis. It circulates in the blood as a zymogen which is later converted to an active form by factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of factor VII, a heavy chain with a catalytic domain and a light chain with 2 EGF-like domains are generated, and the two chains are held together by a disulfide bond. The presence of factor III and calcium ions further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of factor VII results in 2 transcripts. Defects in coagulation factor VII can cause coagulopathy. Coagulation factor VII initiates the extrinsic pathway of blood coagulation. Minor proteolysis converts factor VII to factor VIIa by factors Xa, XIIa, IXa, or thrombin. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium.
-
Synonyms
Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Factor-VIIa although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIIa should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Factor-VIIa in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SNCA E46K, HumanDescription:
Alpha-Synuclein E46K Human Recombinant
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
Product # :
PRO-2626Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNCA E46K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140a.a.) and having a molecular mass of 14.4kDa.SNCA is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
SNCA or Alpha-synuclein is a protein with undisclosed function that mainly concentrated in the brain tissue, mainly in the tips of the neurons in the presynaptic terminals. Almost 1% of the proteins in the brain tissues are synucleins. The protein is located mainly in the hippocampus, thalamus, cerebellum & neocortex. Smaller amounts of the SNCA protein can be found in the neuroglial cells. The MITF protein regulates the SNCA expression in melanocytic cells.
-
Synonyms
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
-
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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKKGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
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 :
ELOB MouseDescription:
Elongin B Mouse Recombinant
Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.
Product # :
PRO-2550Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ELOB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 141 amino acids ( 1-118 a.a.) having a molecular mass of 15.6 kDa. The Recombinant Mouse ELOB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains PBS pH-7.4 containing 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.
-
Synonyms
Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.
-
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 MGSMDVFLMI RRHKTTIFTD AKESSTVFEL KRIVEGILKR PPEEQRLYKD DQLLDDGKTL GECGFTSQTA RPQAPATVGL AFRADDTFEA LRIEPFSSPP ELPDVMKPQD SGGSANEQAV Q
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 :
NME4 Human, ActiveDescription:
Non-Metastatic Cells 4 Human Recombinant, BioActive
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
Product # :
PRO-2642Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
NME4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa.NME4 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME4 solution (0.5mg/ml) contains 40% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 120unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
More Info
-
Introduction
Non-Metastatic Cells 4 or NME4, is a nucleoside diphosphate kinase located in the mitochondria, and is part of the NDK family of proteins. NME4 ais a very common enzyme that enhances transfer of gamma-phosphates, through a phosphohistidine as a intermediate, between dioxynucleoside tri- and diphosphates. NME4 is originated from the nm23 gene. NME4 has a crucial part in the creation of nucleoside triphosphates that are not ATP.
-
Synonyms
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
-
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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA
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 :
Epoetin Human, Sf9Description:
Erythropoietin-alpha Human Recombinant, Sf9
Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.
Product # :
CYT-934Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- sds-page
Description
Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
EPO a protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.sds-page
More Info
-
Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
-
Synonyms
Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.
-
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
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.
-
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 19.5kDa.
What is the source or expression system of EPOETIN Protein?
Sf9, Insect cells.
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.
What is the amino acid sequence of EPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EIF4E HumanDescription:
Eukaryotic Translation Initiation Factor 4E Human Recombinant
CBP, EIF4E1, EIF4EL1, EIF4F.
Product # :
PRO-530Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.
-
Synonyms
CBP, EIF4E1, EIF4EL1, EIF4F.
-
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 MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.
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 :
MORC3 HumanDescription:
MORC Family CW-Type Zinc Finger 3 Human Recombinant
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
Product # :
PRO-2674Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human MORC Family CW-Type Zinc Finger 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 122kDa. MORC3 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MORC3 is supplied in 20mM Sodium phosphate, pH 7.6, 500mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
MORC Family CW-Type Zinc Finger 3 (MORC3) localizes to the nuclear matrix. MORC3 takes part in the regulation of the tumor suppressor protein p53. MORC3may indicate on dermatomyositis (DM) as autoantibodies against this protein have been found in patients.
-
Synonyms
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
-
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. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgG-type human auto-antibodies.2. immunodot test with positive/negative samples.
-
Applications
Western blot with patient sample.
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 :
Myostatin HumanDescription:
Myostatin Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-418Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.More Info
-
Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
-
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Myostatin in sterile 20mM HCl at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Phe-Gly-Leu-Asp.
-
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 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 Myostatin 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 :
Leptin ProteinDescription:
Leptin Human Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-228Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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 :
LGALS2 Mouse, ActiveDescription:
Galectin-2, BioActive Mouse Recombinant
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Product # :
CYT-1155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
More Info
-
Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
-
Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
-
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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
-
Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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.
- View Data Sheet
Name :
MTHFS HumanDescription:
5,10-Methenyltetrahydrofolate Synthetase Human Recombinant
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
Product # :
ENZ-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).
-
Synonyms
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA
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 :
StreptavidinDescription:
Streptavidin Recombinant
Product # :
PRO-791Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.
Source
Escherichia Coli.
Formulation
Lyophilized in 10mM potassium phosphate buffer pH 6.5.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC.
More Info
-
Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.
-
Solubility
It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS. -
Proteolytic Activity
< 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).
-
Specific Activity
> 17U/mg (one unit binds 1 μg D-biotin).
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 :
GFAP HumanDescription:
Glial Fibrillary Acidic Protein Human Recombinant
Glial fibrillary acidic protein, GFAP
Product # :
PRO-2802Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
GFAP Human produced in E.coli is a single, non-glycosylated polypeptide chain (60-383 a.a.) and having a molecular mass of 37906 Dalton.
Source
Escherichia Coli.
Formulation
GFAP was lyophilized from 50mM Tris-HCl pH-7.5, 4M Urea 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Glial fibrillary acidic protein, GFAP
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GFAP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glial Fibrillary Acidic Protein should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized GFAP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Glial Fibrillary Acidic Protein (GFAP), a key intermediate filament protein predominantly found in astrocytes, plays a fundamental role in the central nervous system. Initially recognized for its structural functions, GFAP has emerged as a multifaceted molecule with implications in neural development, synaptic plasticity, and various neurological disorders. This research delves into the realm of GFAP human recombinant protein, shedding light on its structural properties, physiological significance, and its diverse roles in both health and disease.
Structural Complexity of GFAP:
GFAP belongs to the family of intermediate filament proteins, conferring structural support to astrocytes. Its unique structure comprises a central α-helical rod domain flanked by non-helical head and tail domains. This structural complexity allows GFAP to form stable filaments, providing structural integrity to astrocytes and contributing to the architecture of the central nervous system.
Physiological Functions in Glial Cells:
Beyond its structural role, GFAP participates in various physiological processes within glial cells. It is involved in the regulation of astrocyte morphology, motility, and migration, crucial for their interactions with neurons and blood vessels. Additionally, GFAP contributes to the formation and maintenance of the blood-brain barrier, highlighting its significance in the brain's homeostasis.
Implications in Neurological Disorders:
Aberrant GFAP expression and aggregation are associated with several neurological disorders. In Alexander disease, a rare neurodegenerative disorder, mutations in the GFAP gene lead to the formation of GFAP aggregates, contributing to disease pathology. Moreover, elevated levels of GFAP in cerebrospinal fluid serve as a biomarker for various neurological conditions, including traumatic brain injury, Alzheimer's disease, and multiple sclerosis, indicating its involvement in the brain's response to injury and neuroinflammation.
GFAP in Neural Regeneration:
Recent studies have unveiled GFAP’s role in neural regeneration and repair processes. In response to brain injury, GFAP-expressing astrocytes become reactive, forming a glial scar that isolates damaged areas. While this scar formation initially limits tissue damage, persistent scar formation can impede neural regeneration. Understanding the dynamics of GFAP expression in reactive astrocytes is crucial for developing therapies that promote neural regeneration following brain injuries or neurodegenerative diseases.
GFAP human recombinant protein, once thought of as a structural element in astrocytes, has proven to be a pivotal player in the complex landscape of glial biology and neurological disorders. Its intricate functions extend beyond providing structural support, encompassing roles in neural development, disease pathology, and tissue repair. As research continues to uncover the nuances of GFAP’s involvement in health and disease, it offers promising avenues for developing targeted therapies and diagnostic tools, emphasizing its significance in the intricate workings of the central nervous system.
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 :
NKp46 HumanDescription:
Natural Cytotoxicity Receptor NKp46 Human Recombinant
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
Product # :
PRO-432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NKp46 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (22-255) and having a molecular mass of 26.6kDa. NKp46 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NKp46 (1mg/ml) contains phosphate buffered saline (pH7.4) & 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.
-
Synonyms
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
-
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
MQQQTLPKPF IWAEPHFMVP KEKQVTICCQ GNYGAVEYQL HFEGSLFAVD RPKPPERINKVKFYIPDMNS RMAGQYSCIY RVGELWSEPS NLLDLVVTEM YDTPTLSVHP GPEVISGEEV TFYCRLDTAT SMFLLLKEGR SSHVQRGYGK VQAEFPLGPV TTAHRGTYRX FGSYNNHAWSFPSEPVKLLV TGDIENTSLA PEDPTFSADT WGTYLLTTET GLQKDHALWD HTAQN.
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 :
ACVRL1 HumanDescription:
Activin A Receptor Type II-Like 1 Human Recombinant
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
Product # :
CYT-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
-
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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
-
Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.
What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.
What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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.
- View Data Sheet
Name :
EIF2S1 HumanDescription:
Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha Human Recombinant
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
Product # :
PRO-845Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF2S1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 38.2 kDa. The EIF2S1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.
-
Synonyms
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
-
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 MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM ERLERENAEV DGDDDAEEME AKAED
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 :
SUMF1 HumanDescription:
Sulfatase Modifying Factor 1 Human Recombinant
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
Product # :
PRO-986Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SUMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (91-374 a.a.) and having a molecular mass of 34.1kDa.SUMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2M UREA, 2mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.
-
Synonyms
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
-
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 MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE TSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD
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 :
EIF4EBP1 HumanDescription:
Eukaryotic translation initiation factor 4E-binding protein 1 Human Recombinant
Eukaryotic translation initiation factor 4E-binding protein 1, eIF4E-binding protein 1, 4E-BP1, PHAS-I, EIF4EBP1, BP-1, 4EBP1, MGC4316.
Product # :
PRO-532Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF4EBP1 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 138 amino acids (1-118 a.a.) and having a molecular mass of 14.7kDa (molecular weight on SDS-PAGE will appear higher).The EIF4EBP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF4EBP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
EIF4EBP1 (eukaryotic translation initiation factor 4E-binding protein 1) belongs to a family of translation repressor proteins. EIF4EBP1 regulates eIF4E (eukaryotic translation initiation factor 4E) activity by preventing its assembly into the eIF4F complex and mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. EIF4EBP1 is phosphorylated in response to various signals including UV irradiation, resulting in its dissociation from eIF4E and activation of mRNA translation. EIF4EBP1 C-terminus has domains which control function and phosphorylation. EIF4EBP1 has a role in progression of breast neoplasms through cell signaling.
-
Synonyms
Eukaryotic translation initiation factor 4E-binding protein 1, eIF4E-binding protein 1, 4E-BP1, PHAS-I, EIF4EBP1, BP-1, 4EBP1, MGC4316.
-
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 MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN SPEDKRAGGE ESQFEMDI.
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 :
NMM HumanDescription:
Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant
Non-Muscle Myosin-II Regulatory Light Chain, NMM.
Product # :
PRO-366Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant full length expressed in E.coli.The NMM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMM protein at 0.2mg/ml in 20mM HEPES-KOH, pH7, 50mM NaCl, 1mM EDTA and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Assayed for phosphorilation by MLCK.
More Info
-
Introduction
Non muscle Myosins are required for cytokinesis at the end of cell division, when a contractile ring near the plasmalemma divides the cytoplasm of the daughter cells. They are involved in cytoplasmic streaming movements in tissues, and especially in activation of motile cells such as fibroblasts and macrophages. Activation of non-muscle myosin-II is achieved by phosphorylation of Ser33 in the motif KKRPQRATSN by a dedicated, Ca +2 Calmodulin regulated light chain kinase (MLCK).
-
Synonyms
Non-Muscle Myosin-II Regulatory Light Chain, NMM.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
-
Amino Acid Sequence
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD.
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.