Search: 1000 results found for "chikungunya"

Description:

Calponin 2 Human Recombinant

Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-2.

Product # :

PRO-1882

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CNN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131 a.a) and having a molecular mass of 16.9kDa.CNN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.
Synonyms
Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSTQFN KGPSYGLSAE VKNRLLSKYD PQKEAELRTW IEGLTGLSIG PDFQKGLKDG TILCTLMNKL QPGSVPKINR SMQNWHQLEN LSNFIKAMVS YGMNPVDLFE ANDLFESGNM TQVQVSLLAL AGKA

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

Description:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2)

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

Product # :

CHM-271

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Monocyte Chemotactic Protein-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 8.6kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCL2 was lyophilized from a concentrated (1mg/ml) sterile solution without any additives.

Purity

Greater than 98.0% as determined by RP-HPLC and SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

More Info

Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 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 Monocyte Chemotactic Protein-1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN Protein?
CCL2 HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of CCL2 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL2 HUMAN Protein?
CCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN Protein?
The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

What is the amino acid sequence of CCL2 HUMAN Protein?
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

What applications can CCL2 HUMAN Protein be used in?
CCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 HUMAN Protein?
The endotoxin level is minimal, CCL2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL2 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Complexin-1 Human Recombinant

CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

Product # :

PRO-645

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CPLX1 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 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

Purity

Greater than 90% by SDS-PAGE.

More Info

Introduction
CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.
Synonyms
CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.
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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.

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

Description:

Ring Finger Protein 34 Human Recombinant

Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.

Product # :

PRO-1761

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

RNF34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.2kDa.RNF34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RNF34 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Ring Finger Protein 34 (RNF34) has E3 ubiquitin-protein ligase activity. RNF34 has a RINF finger, a motif recognized to be involved in protein-protein and protein-DNA interactions. RNF34 regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. In addition, RNF34 protects cells against apoptosis induced by TNF. RNF34 also binds phosphatidylinositol 5-phosphateand phosphatidylinositol 3-phosphate. Alternatively splicing results in multiple transcript variants encoding distinct isoforms.
Synonyms
Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGS MRKAGAT SMWASCCGLL NEVMGTGAVR GQQSAFAGAT GPFRFTPNPE FSTYPPAATE GPNIVCKACG LSFSVFRKKH VCCDCKKDFC SVCSVLQENL RRCSTCHLLQ ETAFQRPQLM RLKVKDLRQY LILRNIPIDT CREKEDLVDL VLCHHGLGSE DDMDTSSLNS SRSQTSSFFT RSFFSNYTAP SATMSSFQGE LMDGDQTSRS GVPAQVQSEI TSANTEDDDD DDDEDDDDEE ENAEDRNPGL SKERVRASLS DLSSLDDVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV NRLYKENEEN QKSYGERLQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC PICRQYVVRA VHVFKS

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

Description:

Brain-Derived Neurotrophic Factor Human Recombinant, CHO

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-1262

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
sds-page
Citations

Description

Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells

Formulation

The protein was lyophilized with 5% trehalose and 1x PBS

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

sds-page

More Info

Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
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.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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?
CHO Cells

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?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

What is the amino acid sequence of BDNF Protein?
HSDPARRGE 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.
References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication

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

Description:

Stromal Cell-Derived Factor 2, Sf9 Human Recombinant

Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2

Product # :

CHM-034

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SDF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (19-211a.a.) and having a molecular mass of 22.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDF2 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SDF2 protein solution (0.25mg/ml) contains 50mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl 0.1mM PMSF and 0.5mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2 is a protein-coding gene whose alternative splicing results in coding and non-coding variants.
Synonyms
Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH
Background
What is the molecular weight/Mw of SDF2 HUMAN, SF9 Protein?
SDF2 HUMAN, SF9 Protein has a total Mw of 22.3kDa.

What is the source or expression system of SDF2 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of SDF2 HUMAN, SF9 Protein?
SDF2 HUMAN, SF9 Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of SDF2 HUMAN, SF9 Protein?
The biological functionality of SDF2 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of SDF2 HUMAN, SF9 Protein?
ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH

What applications can SDF2 HUMAN, SF9 Protein be used in?
SDF2 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for SDF2 HUMAN, SF9 Protein?
The endotoxin level is minimal, SDF2 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies SDF2 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of SDF2 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Neurogenin 3 Human Recombinant

Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

Product # :

CYT-811

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NEUROG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-214) and having a molecular mass of 25.1 kDa. NEUROG3 is fused to a 20 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The NEUROG3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
NEUROG3 is a common helix-loop-helix (bHLH) transcription factor which takes part in neurogenesis. NEUROG3 functions as a heterodimer with another bHLH protein. Mutations in this gene can result in congenital malabsorptive diarrhea 4 (DIAR4).
Synonyms
Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.
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 MTPQPSGAPT VQVTRETERS FPRASEDEVT CPTSAPPSPT RTRGNCAEAE EGGCRGAPRK LRARRGGRSR PKSELALSKQ RRSRRKKAND RERNRMHNLN SALDALRGVL PTFPDDAKLT KIETLRFAHN YIWALTQTLR IADHSLYALE PPAPHCGELG SPGGSPGDWG SLYSPVSQAG SLSPAASLEE RPGLLGATSS ACLSPGSLAF SDFL

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

Description:

Age-Related Maculopathy Susceptibility 2 Human Recombinant

Age-related maculopathy susceptibility protein 2, ARMD8

Product # :

PRO-2628

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

ARMS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107a.a.) and having a molecular mass of 13.8kDa.ARMS2 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

ARMS2 protein solution (0.25mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Age-Related Maculopathy Susceptibility 2 or ARMS2 is a protein that is is being researches for its ability to take part in diseases in old age. Mutations in Age-Related Maculopathy Susceptibility 2 is related to age-caused molecular degeneration.
Synonyms
Age-related maculopathy susceptibility protein 2, ARMD8
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 MGSMLRLYPG PMVTEAEGKG GPEMASLSSS VVPVSFISTL RESVLDPGVG GEGASDKQRS KLSLSHSMIP AAKIHTELCL PAFFSPAGTQ RRFQQPQHHL TLSIIHTAAR

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

Description:

Sparc/Osteonectin 3 Mouse Recombinant

Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

Product # :

PRO-2328

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH 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.

Description:

8-Oxoguanine DNA Glycosylase Mouse Recombinant

HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.

Product # :

ENZ-1048

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

OGG1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 41.3kDa. OGG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OGG1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.
Synonyms
HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.
Physical Appearance
Sterile filtered colourless 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 MGSMLFRSWL PSSMRHRTLS SSPALWASIP CPRSELRLDL VLASGQSFRW KEQSPAHWSG VLADQVWTLT QTEDQLYCTV YRGDDSQVSR PTLEELETLH KYFQLDVSLA QLYSHWASVD SHFQRVAQKF QGVRLLRQDP TECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPNLHAL AGPEAETHLR KLGLGYRARY VRASAKAILE EQGGPAWLQQ LRVAPYEEAH KALCTLPGVG AKVADCICLM ALDKPQAVPV DVHVWQIAHR DYGWHPKTSQ AKGPSPLANK ELGNFFRNLW GPYAGWAQAV LFSADLRQPS LSREPPAKRK KGSKRPEG.

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

Description:

Phosphate Cytidylyltransferase 2 Human Recombinant

MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.

Product # :

ENZ-221

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PCYT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389) and having a molecular mass of 45.9kDa.PCYT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PCYT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
PCYT2 is a member of the cytidylyltransferase family. PCYT2 is an enzyme which catalyzes the formation of CDP-MEA from CTP and phospho MEA in the Kennedy pathway of phospholipid synthesis. PCYT2 has the strongest expression in the liver, heart, and skeletal muscle.
Synonyms
MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.
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 MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF.

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

Description:

Interleukin-2 Feline Recombinant

Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.

Product # :

CYT-1018

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
SDS-PAGE
Citations

Description

IL2 Feline Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids (21-154 a.a) and having a molecular mass of 17.8kDa. IL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL2 protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is less or equal to 0.3ng/ml.

SDS-PAGE

More Info

Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.
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 MGSAPASSST KETQQQLEQL LLDLRLLLNG VNNPENPKLS RMLTFKFYVP KKATELTHLQ CLVEELKPLE EVLYLAQSKN FHLNHIKELM SNINVTVLKL KGSETRFTCN YDDETATIVE FLNKWITFCQ SIFSTLT.
Background
What is the molecular weight/Mw of IL 2 FELINE Protein?
L 2 FELINE Protein has a total Mw of 17.8kDa.

What is the source or expression system of IL 2 FELINE Protein?
Escherichia Coli.

What is the Purity of IL 2 FELINE Protein?
IL 2 FELINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 FELINE Protein?
Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is less or equal to 0.3ng/ml.

What is the amino acid sequence of IL 2 FELINE Protein?
MGSSHHHHHH SSGLVPRGSH MGSAPASSST KETQQQLEQL LLDLRLLLNG VNNPENPKLS RMLTFKFYVP KKATELTHLQ CLVEELKPLE EVLYLAQSKN FHLNHIKELM SNINVTVLKL KGSETRFTCN YDDETATIVE FLNKWITFCQ SIFSTLT.

What applications can IL 2 FELINE Protein be used in?
IL 2 FELINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 FELINE Protein?
The endotoxin level is minimal, IL 2 FELINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 FELINE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 2 FELINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Cathelicidin Antimicrobial Peptide Human Recombinant

CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

Product # :

PRO-1405

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

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

Description:

Cyclin-Dependent Kinase Inhibitor 1A Human Recombinant

Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

Product # :

PKA-043

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CDKN1A Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (1-164) and having a molecular mass of 20.2 kDa.CDKN1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDKN1A solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 0.1M NaCl and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.
Synonyms
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
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 MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP.

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

Description:

Queuine TRNA-Ribosyltransferase 1 Human Recombinant

Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.

Product # :

ENZ-877

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

QTRT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-403 a.a) and having a molecular mass of 46.7kDa. QTRT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

QTRT1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Queuine TRNA-Ribosyltransferase 1 also known as QTRT1 is a member of the queuine tRNA-ribosyltransferase family. QTRT1 interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. Furthermore, QTRT1 exchanges queuine for the guanine at the wobble position of tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), in this manner forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Synonyms
Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.
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 MGSEFMAGAA TQASLESAPR IMRLVAECSR SRARAGELWL PHGTVATPVF MPVGTQATMK GITTEQLDAL GCRICLGNTY HLGLRPGPEL IQKANGLHGF MNWPHNLLTD SGGFQMVSLV SLSEVTEEGV RFRSPYDGNE TLLSPEKSVQ IQNALGSDII MQLDDVVSST VTGPRVEEAM YRSIRWLDRC IAAHQRPDKQ NLFAIIQGGL DADLRATCLE EMTKRDVPGF AIGGLSGGES KSQFWRMVAL STSRLPKDKP RYLMGVGYAT DLVVCVALGC DMFDCVFPTR TARFGSALVP TGNLQLRKKV FEKDFGPIDP ECTCPTCQKH SRAFLHALLH SDNTAALHHL TVHNIAYQLQ LMSAVRTSIV EKRFPDFVRD FMGAMYGDPT LCPTWATDAL ASVGITLG.

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

Description:

Microtubule-Associated Protein Tau 412 a.a. Human Recombinant

Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

Product # :

PRO-210

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

MAPT Human Recombinant (Isoform 5) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 45.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.
Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS KCGSKDNIKH VPGGGSVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.

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

Description:

Vacuolar Protein Sorting 26A Human Recombinant

Vacuolar protein sorting-associated protein 26A, Vesicle protein sorting 26A, hVPS26, VPS26A, VPS26, HB58, PEP8A, Hbeta58.

Product # :

PRO-1161

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

VPS26A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 40.6kDa.VPS26A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

VPS26A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Vacuolar protein sorting-associated protein 26A (VPS26A) is a vital element of the retromer complex, which is required to recover lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Furthermore, VPS26A is essential in the regulation of transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Expression analysis in yeast and mammalian cells reveal that VPS26A interacts directly with VPS35 that functions as the core of the retromer complex.
Synonyms
Vacuolar protein sorting-associated protein 26A, Vesicle protein sorting 26A, hVPS26, VPS26A, VPS26, HB58, PEP8A, Hbeta58.
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 MGSMSFLGGF FGPICEIDIV LNDGETRKMA EMKTEDGKVE KHYLFYDGES VSGKVNLAFK QPGKRLEHQG IRIEFVGQIE LFNDKSNTHE FVNLVKELAL PGELTQSRSY DFEFMQVEKP YESYIGANVR LRYFLKVTIV RRLTDLVKEY DLIVHQLATY PDVNNSIKME VGIEDCLHIE FEYNKSKYHL KDVIVGKIYF LLVRIKIQHM ELQLIKKEIT GIGPSTTTET ETIAKYEIMD GAPVKGESIP IRLFLAGYDP TPTMRDVNKK FSVRYFLNLV LVDEEDRRYF KQQEIILWRK APEKLRKQRT NFHQRFESPE SQASAEQPEM.

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

Description:

Zinc Finger, Matrin-Type 3 Human Recombinant

Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.

Product # :

PRO-1635

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

ZMAT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 312 amino acids (1-289) and having a molecular mass of 34.4kDa.ZMAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ZMAT3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
ZMAT3 is a protein with a nuclear localization signal and 3 zinc finger domains. The mRNA and the protein of this gene are upregulated by wildtype p53. When overexpressed, ZMAT3 can produce tumor cell growth, indicating that ZMAT3 takes part in the p53-dependent growth regulatory pathway. Alternative splicing of ZMAT3 produce two transcript variants encoding two isoforms differing in only one amino acid.
Synonyms
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
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 MGSMILLQHA VLPPPKQPSP SPPMSVATRS TGTLQLPPQK PFGQEASLPL AGEEELSKGG EQDCALEELC KPLYCKLCNV TLNSAQQAQA HYQGKNHGKK LRNYYAANSC PPPARMSNVV EPAATPVVPV PPQMGSFKPG GRVILATEND YCKLCDASFS SPAVAQAHYQ GKNHAKRLRL AEAQSNSFSE SSELGQRRAR KEGNEFKMMP NRRNMYTVQN NSAGPYFNPR SRQRIPRDLA MCVTPSGQFY CSMCNVGAGE EMEFRQHLES KQHKSKVSEQ RYRNEMENLG YV

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

Description:

Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant

Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

Product # :

PRO-258

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HIF1A Human (0.25mg/ml) solution containing 20mM Tris buffer(pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl and 1mM EDTA.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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 MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.

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

Description:

Mitogen-Activated Protein Kinase 11 Human Recombinant

Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.

Product # :

PKA-013

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

MAPK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-364 a.a.) and having a molecular mass of 43.8kDa.MAPK11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAPK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2mM DTT, 100mM NaCl and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE analysis.

More Info

Introduction
MAPK11 belongs to the MAP kinase family and is most associated with p38 MAP kinases (MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. MAPK11 cooperates with HDAC3 and Promyelocytic leukemia protein and takes part in a signal transduction pathway which is activated by alterations in the osmolarity of the extracellular environment, by environmental stress, or by cytokines.
Synonyms
Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.
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 MGSMSGPRAG FYRQELNKTV WEVPQRLQGL RPVGSGAYGS VCSAYDARLR QKVAVKKLSR PFQSLIHARR TYRELRLLKH LKHENVIGLL DVFTPATSIE DFSEVYLVTT LMGADLNNIV KCQALSDEHV QFLVYQLLRG LKYIHSAGII HRDLKPSNVA VNEDCELRIL DFGLARQADE EMTGYVATRW YRAPEIMLNW MHYNQTVDIW SVGCIMAELL QGKALFPGSD YIDQLKRIME VVGTPSPEVL AKISSEHART YIQSLPPMPQ KDLSSIFRGA NPLAIDLLGR MLVLDSDQRV SAAEALAHAY FSQYHDPEDE PEAEPYDESV EAKERTLEEW KELTYQEVLS FKPPEPPKPP GSLEIEQ.

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

Description:

Ciliary-Neurotrophic Factor Human Recombinant

HCNTF, CNTF, Ciliary Neurotrophic Factor.

Product # :

CYT-272

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

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-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

More Info

Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 HCNTF in sterile 18MΩ-cm H2O 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 Met-Ala-Phe-Thr-Glu.
Background
Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications
Abstract:
Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.
Introduction:
CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.
Mechanisms of Action:
CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.
Production Methods:
Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.
Therapeutic Applications:
CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.
Challenges and Future Directions:
While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.
Conclusion:
Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.

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

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

What is the Biological Activity of CNTF Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

What is the amino acid sequence of CNTF Protein?
CNTF Protein is composed from 199 amino acids.

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

What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
Protein content
CNTF quantitation was carried out by two independent methods1. 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). 2. Analysis by RP-HPLC, using a standard solution of CNTF Recombinant as a Reference Standard.

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

Description:

Carcinoembryonic Antigen Human

CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

Product # :

PRO-2801

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

Source

Liver tissue.

Formulation

CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Applications
Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.
Background
Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.
Structural Complexity of CEA:
CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.
CEA in Cancer Biology:
CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.
Beyond Cancer: CEA in Development and Inflammation:
While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.
CEA as a Diagnostic and Therapeutic Target:
The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

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

Description:

Charged Multivesicular Body Protein 6 Human Recombinant

Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.

Product # :

PRO-1085

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CHMP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-201 a.a) and having a molecular mass of 26.1kDa (Molecular size on SDS-PAGE will appear higher).CHMP6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CHMP6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Charged multivesicular body protein 6 (CHMP6) is a member of the SNF7 family. The CHMP6 protein is a core component of the endosomal sorting necessary for transport complex III (ESCRT-III) that is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) which are produced by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes facilitating degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.
Synonyms
Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.
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 MGSHMGNLFG RKKQSRVTEQ DKAILQLKQQ RDKLRQYQKR IAQQLERERA LARQLLRDGR KERAKLLLKK KRYQEQLLDR TENQISSLEA MVQSIEFTQI EMKVMEGLQF GNECLNKMHQ VMSIEEVERI LDETQEAVEY QRQIDELLAG SFTQEDEDAI LEELSAITQE QIELPEVPSE PLPEKIPENV PVKARPRQAE LVAAS.

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

Description:

Interferon-alpha Neutralizing, Mouse Anti-Human

Product # :

ANT-122

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

formulation
More Info
Citations

Formulation

1mg/ml in PBS (after reconstitution).

More Info

Introduction
IFN-alpha is produced by macrophages, IFN-alpha has antiviral activities and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IFN Alpha.
Ig Subclass
Mouse IgG1.
Clone
NYRhIFN-A (neut).
Applications
Direct ELISA (Does not work in Western Blotting). This is a Neutralizing antibody.
Note
The antibody can be used for Capture ELISA together with ProSpec’s Mouse Anti Human IFN-alpha Western Blot antibody.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange.

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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

sds-page

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity